메뉴 건너뛰기




Volumn 59, Issue 21, 2016, Pages 9599-9621

Therapeutic potential of foldamers: From chemical biology tools to drug candidates?

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANTIBIOTIC AGENT; ANTINEOPLASTIC AGENT; BETA AMINO ACID; CELL PENETRATING PEPTIDE; CHOLESTEROL; DRUG; FOLDAMER; GAMMA AMINO ACID; HYPOXIA INDUCIBLE FACTOR 1; LUNG SURFACTANT PROTEIN; OLIGOMER; PEPTIDE HORMONE; PEPTOID; PIPERAZINE DERIVATIVE; POLYSACCHARIDE SULFATE; PROTEIN; PROTEIN BCL 2; UNCLASSIFIED DRUG; UREA; PEPTIDE; POLYCYCLIC AROMATIC HYDROCARBON;

EID: 84994852259     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/acs.jmedchem.6b00376     Document Type: Article
Times cited : (131)

References (214)
  • 1
    • 79956128878 scopus 로고    scopus 로고
    • Synthetic Foldamers
    • Guichard, G.; Huc, I. Synthetic Foldamers Chem. Commun. 2011, 47, 5933-5941 10.1039/c1cc11137j
    • (2011) Chem. Commun. , vol.47 , pp. 5933-5941
    • Guichard, G.1    Huc, I.2
  • 2
    • 83455254495 scopus 로고    scopus 로고
    • Peptidic Foldamers: Ramping up Diversity
    • Martinek, T. A.; Fülöp, F. Peptidic Foldamers: Ramping up Diversity Chem. Soc. Rev. 2012, 41, 687-702 10.1039/C1CS15097A
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 687-702
    • Martinek, T.A.1    Fülöp, F.2
  • 3
    • 84946500622 scopus 로고    scopus 로고
    • An Overview of Peptide and Peptoid Foldamers in Medicinal Chemistry
    • Mándity, I. M.; Fülöp, F. An Overview of Peptide and Peptoid Foldamers in Medicinal Chemistry Expert Opin. Drug Discovery 2015, 10, 1163-1177 10.1517/17460441.2015.1076790
    • (2015) Expert Opin. Drug Discovery , vol.10 , pp. 1163-1177
    • Mándity, I.M.1    Fülöp, F.2
  • 4
    • 83455201294 scopus 로고    scopus 로고
    • Peptide and Peptoid Foldamers in Medicinal Chemistry
    • Horne, W. S. Peptide and Peptoid Foldamers in Medicinal Chemistry Expert Opin. Drug Discovery 2011, 6, 1247-1262 10.1517/17460441.2011.632002
    • (2011) Expert Opin. Drug Discovery , vol.6 , pp. 1247-1262
    • Horne, W.S.1
  • 5
    • 0542421525 scopus 로고    scopus 로고
    • Foldamers: A Manifesto
    • Gellman, S. H. Foldamers: A Manifesto Acc. Chem. Res. 1998, 31, 173-180 10.1021/ar960298r
    • (1998) Acc. Chem. Res. , vol.31 , pp. 173-180
    • Gellman, S.H.1
  • 6
    • 84937518958 scopus 로고    scopus 로고
    • Structure-Based Design of Inhibitors of Protein-Protein Interactions: Mimicking Peptide Binding Epitopes
    • Pelay-Gimeno, M.; Glas, A.; Koch, O.; Grossmann, T. N. Structure-Based Design of Inhibitors of Protein-Protein Interactions: Mimicking Peptide Binding Epitopes Angew. Chem., Int. Ed. 2015, 54, 8896-8927 10.1002/anie.201412070
    • (2015) Angew. Chem., Int. Ed. , vol.54 , pp. 8896-8927
    • Pelay-Gimeno, M.1    Glas, A.2    Koch, O.3    Grossmann, T.N.4
  • 8
    • 0030800453 scopus 로고    scopus 로고
    • Studying the Stability of a Helical β-Heptapeptide by Molecular Dynamics Simulations
    • Daura, X.; van Gunsteren, W. F.; Rigo, D.; Jaun, B.; Seebach, D. Studying the Stability of a Helical β-Heptapeptide by Molecular Dynamics Simulations Chem.-Eur. J. 1997, 3, 1410-1417 10.1002/chem.19970030907
    • (1997) Chem. - Eur. J. , vol.3 , pp. 1410-1417
    • Daura, X.1    Van Gunsteren, W.F.2    Rigo, D.3    Jaun, B.4    Seebach, D.5
  • 9
    • 0027975871 scopus 로고
    • Intramolecular Hydrogen Bonding in Derivatives of.beta.-Alanine and.gamma.-Amino Butyric Acid; Model Studies for the Folding of Unnatural Polypeptide Backbones
    • Dado, G. P.; Gellman, S. H. Intramolecular Hydrogen Bonding in Derivatives of.beta.-Alanine and.gamma.-Amino Butyric Acid; Model Studies for the Folding of Unnatural Polypeptide Backbones J. Am. Chem. Soc. 1994, 116, 1054-1062 10.1021/ja00082a029
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 1054-1062
    • Dado, G.P.1    Gellman, S.H.2
  • 10
    • 0030461803 scopus 로고    scopus 로고
    • β-Peptide Foldamers: Robust Helix Formation in a New Family of β-Amino Acid Oligomers
    • Appella, D. H.; Christianson, L. A.; Karle, I. L.; Powell, D. R.; Gellman, S. H. β-Peptide Foldamers: Robust Helix Formation in a New Family of β-Amino Acid Oligomers J. Am. Chem. Soc. 1996, 118, 13071-13072 10.1021/ja963290l
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 13071-13072
    • Appella, D.H.1    Christianson, L.A.2    Karle, I.L.3    Powell, D.R.4    Gellman, S.H.5
  • 11
    • 0032544937 scopus 로고    scopus 로고
    • Destabilization of the 310-Helix in Peptides Based on Cα-Tetrasubstituted α-Amino Acids by Main-Chain to Side-Chain Hydrogen Bonds
    • Wolf, W. M.; Stasiak, M.; Leplawy, M. T.; Bianco, A.; Formaggio, F.; Crisma, M.; Toniolo, C. Destabilization of the 310-Helix in Peptides Based on Cα-Tetrasubstituted α-Amino Acids by Main-Chain to Side-Chain Hydrogen Bonds J. Am. Chem. Soc. 1998, 120, 11558-11566 10.1021/ja982194c
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11558-11566
    • Wolf, W.M.1    Stasiak, M.2    Leplawy, M.T.3    Bianco, A.4    Formaggio, F.5    Crisma, M.6    Toniolo, C.7
  • 12
    • 57349134690 scopus 로고    scopus 로고
    • Foldamers with Heterogeneous Backbones
    • Horne, W. S.; Gellman, S. H. Foldamers with Heterogeneous Backbones Acc. Chem. Res. 2008, 41, 1399-1408 10.1021/ar800009n
    • (2008) Acc. Chem. Res. , vol.41 , pp. 1399-1408
    • Horne, W.S.1    Gellman, S.H.2
  • 15
    • 9444226868 scopus 로고    scopus 로고
    • The World of β- And γ-Peptides Comprised of Homologated Proteinogenic Amino Acids and Other Components
    • Seebach, D.; Beck, A. K.; Bierbaum, D. J. The World of β- and γ-Peptides Comprised of Homologated Proteinogenic Amino Acids and Other Components Chem. Biodiversity 2004, 1, 1111-1239 10.1002/cbdv.200490087
    • (2004) Chem. Biodiversity , vol.1 , pp. 1111-1239
    • Seebach, D.1    Beck, A.K.2    Bierbaum, D.J.3
  • 16
    • 76649129844 scopus 로고    scopus 로고
    • Peptoid-Peptide Hybrid Backbone Architectures
    • Olsen, C. A. Peptoid-Peptide Hybrid Backbone Architectures ChemBioChem 2010, 11, 152-160 10.1002/cbic.200900618
    • (2010) ChemBioChem , vol.11 , pp. 152-160
    • Olsen, C.A.1
  • 19
    • 84908374024 scopus 로고    scopus 로고
    • Protein Backbone Engineering as a Strategy to Advance Foldamers Toward the Frontier of Protein-like Tertiary Structure
    • Reinert, Z. E.; Horne, W. S. Protein Backbone Engineering as a Strategy to Advance Foldamers Toward the Frontier of Protein-like Tertiary Structure Org. Biomol. Chem. 2014, 12, 8796-8802 10.1039/C4OB01769B
    • (2014) Org. Biomol. Chem. , vol.12 , pp. 8796-8802
    • Reinert, Z.E.1    Horne, W.S.2
  • 20
    • 84919347025 scopus 로고    scopus 로고
    • Heterogeneous Foldamers from Aliphatic-Aromatic Amino Acid Building Blocks: Current Trends and Future Prospects
    • Nair, R. V.; Vijayadas, K. N.; Roy, A.; Sanjayan, G. J. Heterogeneous Foldamers from Aliphatic-Aromatic Amino Acid Building Blocks: Current Trends and Future Prospects Eur. J. Org. Chem. 2014, 2014, 7763-7780 10.1002/ejoc.201402877
    • (2014) Eur. J. Org. Chem. , vol.2014 , pp. 7763-7780
    • Nair, R.V.1    Vijayadas, K.N.2    Roy, A.3    Sanjayan, G.J.4
  • 21
    • 84867355275 scopus 로고    scopus 로고
    • Aromatic Amide Foldamers: Structures, Properties, and Functions
    • Zhang, D.-W.; Zhao, X.; Hou, J.-L.; Li, Z.-T. Aromatic Amide Foldamers: Structures, Properties, and Functions Chem. Rev. 2012, 112, 5271-5316 10.1021/cr300116k
    • (2012) Chem. Rev. , vol.112 , pp. 5271-5316
    • Zhang, D.-W.1    Zhao, X.2    Hou, J.-L.3    Li, Z.-T.4
  • 22
    • 75449102744 scopus 로고    scopus 로고
    • De Novo Design of Antimicrobial Polymers, Foldamers, and Small Molecules: From Discovery to Practical Applications
    • Tew, G. N.; Scott, R. W.; Klein, M. L.; DeGrado, W. F. De Novo Design of Antimicrobial Polymers, Foldamers, and Small Molecules: From Discovery to Practical Applications Acc. Chem. Res. 2010, 43, 30-39 10.1021/ar900036b
    • (2010) Acc. Chem. Res. , vol.43 , pp. 30-39
    • Tew, G.N.1    Scott, R.W.2    Klein, M.L.3    DeGrado, W.F.4
  • 23
    • 84875436143 scopus 로고    scopus 로고
    • Inhibition of α-Helix-Mediated Protein-Protein Interactions using Designed Molecules
    • Azzarito, V.; Long, K.; Murphy, N. S.; Wilson, A. J. Inhibition of α-Helix-Mediated Protein-Protein Interactions using Designed Molecules Nat. Chem. 2013, 5, 161-173 10.1038/nchem.1568
    • (2013) Nat. Chem. , vol.5 , pp. 161-173
    • Azzarito, V.1    Long, K.2    Murphy, N.S.3    Wilson, A.J.4
  • 24
    • 0035471135 scopus 로고    scopus 로고
    • Beta-Peptides: From Structure to Function
    • Cheng, R. P.; Gellman, S. H.; DeGrado, W. F. beta-Peptides: From Structure to Function Chem. Rev. 2001, 101, 3219-3232 10.1021/cr000045i
    • (2001) Chem. Rev. , vol.101 , pp. 3219-3232
    • Cheng, R.P.1    Gellman, S.H.2    DeGrado, W.F.3
  • 25
    • 33645289135 scopus 로고    scopus 로고
    • Application of Alicyclic β-Amino Acids in Peptide Chemistry
    • Fülöp, F.; Martinek, T. A.; Tóth, G. K. Application of Alicyclic β-Amino Acids in Peptide Chemistry Chem. Soc. Rev. 2006, 35, 323-334 10.1039/b501173f
    • (2006) Chem. Soc. Rev. , vol.35 , pp. 323-334
    • Fülöp, F.1    Martinek, T.A.2    Tóth, G.K.3
  • 26
    • 84945135157 scopus 로고    scopus 로고
    • Foldamers: Biomimetic and Built to Order
    • Horne, W. S. Foldamers: Biomimetic and Built to Order Nat. Chem. 2015, 7, 858-859 10.1038/nchem.2385
    • (2015) Nat. Chem. , vol.7 , pp. 858-859
    • Horne, W.S.1
  • 27
    • 84918498601 scopus 로고    scopus 로고
    • Peptides Containing β-Amino Acid Patterns: Challenges and Successes in Medicinal Chemistry
    • Cabrele, C.; Martinek, T. A.; Reiser, O.; Berlicki, C. Peptides Containing β-Amino Acid Patterns: Challenges and Successes in Medicinal Chemistry J. Med. Chem. 2014, 57, 9718-9739 10.1021/jm5010896
    • (2014) J. Med. Chem. , vol.57 , pp. 9718-9739
    • Cabrele, C.1    Martinek, T.A.2    Reiser, O.3    Berlicki, C.4
  • 28
    • 78650334402 scopus 로고    scopus 로고
    • Building β-Peptide H10/12 Foldamer Helices with Six-Membered Cyclic Side-Chains: Fine-Tuning of Folding and Self-Assembly
    • Mándity, I. n. M.; Fülöp, L.; Vass, E. r.; Tóth, G. b. K.; Martinek, T. s. A.; Fülöp, F. Building β-Peptide H10/12 Foldamer Helices with Six-Membered Cyclic Side-Chains: Fine-Tuning of Folding and Self-Assembly Org. Lett. 2010, 12, 5584-5587 10.1021/ol102494m
    • (2010) Org. Lett. , vol.12 , pp. 5584-5587
    • Mándity, N.M.1    Fülöp, L.2    Vass, E.R.3    Tóth B G, K.4    Martinek ST, A.5    Fülöp, F.6
  • 29
    • 55549147466 scopus 로고    scopus 로고
    • β-Strand Mimetics: Formation of Bend-Strands in Oligomers of Enantiomeric β-Amino Acids
    • Chandrasekhar, S.; Sudhakar, A.; Kiran, M. U.; Babu, B. N.; Jagadeesh, B. β-Strand Mimetics: Formation of Bend-Strands in Oligomers of Enantiomeric β-Amino Acids Tetrahedron Lett. 2008, 49, 7368-7371 10.1016/j.tetlet.2008.10.031
    • (2008) Tetrahedron Lett. , vol.49 , pp. 7368-7371
    • Chandrasekhar, S.1    Sudhakar, A.2    Kiran, M.U.3    Babu, B.N.4    Jagadeesh, B.5
  • 31
    • 0032569174 scopus 로고    scopus 로고
    • Design of Secondary Structures in Unnatural Peptides: Stable Helical γ-Tetra-, Hexa-, and Octapeptides and Consequences of α-Substitution
    • Hanessian, S.; Luo, X.; Schaum, R.; Michnick, S. Design of Secondary Structures in Unnatural Peptides: Stable Helical γ-Tetra-, Hexa-, and Octapeptides and Consequences of α-Substitution J. Am. Chem. Soc. 1998, 120, 8569-8570 10.1021/ja9814671
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8569-8570
    • Hanessian, S.1    Luo, X.2    Schaum, R.3    Michnick, S.4
  • 33
    • 33750036386 scopus 로고    scopus 로고
    • Effects of the Alternating Backbone Configuration on the Secondary Structure and Self-Assembly of β-Peptides
    • Martinek, T. A.; Mándity, I. M.; Fülöp, L.; Tóth, G. K.; Vass, E.; Hollósi, M.; Forró, E.; Fülöp, F. Effects of the Alternating Backbone Configuration on the Secondary Structure and Self-Assembly of β-Peptides J. Am. Chem. Soc. 2006, 128, 13539-13544 10.1021/ja063890c
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 13539-13544
    • Martinek, T.A.1    Mándity, I.M.2    Fülöp, L.3    Tóth, G.K.4    Vass, E.5    Hollósi, M.6    Forró, E.7    Fülöp, F.8
  • 34
    • 84928963439 scopus 로고    scopus 로고
    • Cis-2-Aminocyclohex-4-enecarboxylic acid as a New Building Block of Helical Foldamers
    • Kwon, S.; Kang, P.; Choi, M.-G.; Choi, S. H. cis-2-Aminocyclohex-4-enecarboxylic acid as a New Building Block of Helical Foldamers New J. Chem. 2015, 39, 3221-3224 10.1039/C4NJ02056A
    • (2015) New J. Chem. , vol.39 , pp. 3221-3224
    • Kwon, S.1    Kang, P.2    Choi, M.-G.3    Choi, S.H.4
  • 35
    • 84887859028 scopus 로고    scopus 로고
    • Structural Characterization of α/β-Peptides having Alternating Residues: X-ray Structures of the 11/9-Helix from Crystals of Racemic Mixtures
    • Lee, M.; Shim, J.; Kang, P.; Guzei, I. A.; Choi, S. H. Structural Characterization of α/β-Peptides having Alternating Residues: X-ray Structures of the 11/9-Helix from Crystals of Racemic Mixtures Angew. Chem., Int. Ed. 2013, 52, 12564-12567 10.1002/anie.201306404
    • (2013) Angew. Chem., Int. Ed. , vol.52 , pp. 12564-12567
    • Lee, M.1    Shim, J.2    Kang, P.3    Guzei, I.A.4    Choi, S.H.5
  • 36
    • 33750999348 scopus 로고    scopus 로고
    • 12/10- and 11/13-Mixed Helices in α/γ- and β/γ-Hybrid Peptides Containing C-Linked Carbo-γ-amino Acids with Alternating α- And β-Amino Acids
    • Sharma, G. V. M; Jadhav, V. B.; Ramakrishna, K. V. S.; Jayaprakash, P.; Narsimulu, K.; Subash, V.; Kunwar, A. C. 12/10- and 11/13-Mixed Helices in α/γ- and β/γ-Hybrid Peptides Containing C-Linked Carbo-γ-amino Acids with Alternating α- and β-Amino Acids J. Am. Chem. Soc. 2006, 128, 14657-14668 10.1021/ja064875a
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 14657-14668
    • Sharma, G.V.M.1    Jadhav, V.B.2    Ramakrishna, K.V.S.3    Jayaprakash, P.4    Narsimulu, K.5    Subash, V.6    Kunwar, A.C.7
  • 38
    • 84962433748 scopus 로고    scopus 로고
    • Helix Formation in α, γ-and β, γ-hybrid Peptides: Theoretical Insights into Mimicry of α-and β-Peptides
    • Baldauf, C.; Günther, R.; Hofmann, H.-J. Helix Formation in α, γ-and β, γ-hybrid Peptides: Theoretical Insights into Mimicry of α-and β-Peptides J. Org. Chem. 2006, 71, 1200-1208 10.1021/jo052340e
    • (2006) J. Org. Chem. , vol.71 , pp. 1200-1208
    • Baldauf, C.1    Günther, R.2    Hofmann, H.-J.3
  • 40
    • 0037014049 scopus 로고    scopus 로고
    • Stable Helical Secondary Structure in Short-Chain N,N′-Linked Oligoureas Bearing Proteinogenic Side Chains
    • Semetey, V.; Rognan, D.; Hemmerlin, C.; Graff, R.; Briand, J.-P.; Marraud, M.; Guichard, G. Stable Helical Secondary Structure in Short-Chain N,N′-Linked Oligoureas Bearing Proteinogenic Side Chains Angew. Chem., Int. Ed. 2002, 41, 1893-1895 10.1002/1521-3773(20020603)41:11<1893::AID-ANIE1893>3.0.CO;2-F
    • (2002) Angew. Chem., Int. Ed. , vol.41 , pp. 1893-1895
    • Semetey, V.1    Rognan, D.2    Hemmerlin, C.3    Graff, R.4    Briand, J.-P.5    Marraud, M.6    Guichard, G.7
  • 41
    • 84875732153 scopus 로고    scopus 로고
    • Controlling Helix Formation in the γ-Peptide Superfamily: Heterogeneous Foldamers with Urea/Amide and Urea/Carbamate Backbones
    • Pendem, N.; Nelli, Y. R.; Douat, C.; Fischer, L.; Laguerre, M.; Ennifar, E.; Kauffmann, B.; Guichard, G. Controlling Helix Formation in the γ-Peptide Superfamily: Heterogeneous Foldamers with Urea/Amide and Urea/Carbamate Backbones Angew. Chem., Int. Ed. 2013, 52, 4147-4151 10.1002/anie.201209838
    • (2013) Angew. Chem., Int. Ed. , vol.52 , pp. 4147-4151
    • Pendem, N.1    Nelli, Y.R.2    Douat, C.3    Fischer, L.4    Laguerre, M.5    Ennifar, E.6    Kauffmann, B.7    Guichard, G.8
  • 42
    • 84938988017 scopus 로고    scopus 로고
    • α-Peptide-Oligourea Chimeras: Stabilization of Short α-Helices by Non-Peptide Helical Foldamers
    • Fremaux, J.; Mauran, L.; Pulka-Ziach, K.; Kauffmann, B.; Odaert, B.; Guichard, G. α-Peptide-Oligourea Chimeras: Stabilization of Short α-Helices by Non-Peptide Helical Foldamers Angew. Chem., Int. Ed. 2015, 54, 9816-9820 10.1002/anie.201500901
    • (2015) Angew. Chem., Int. Ed. , vol.54 , pp. 9816-9820
    • Fremaux, J.1    Mauran, L.2    Pulka-Ziach, K.3    Kauffmann, B.4    Odaert, B.5    Guichard, G.6
  • 44
    • 84939285980 scopus 로고    scopus 로고
    • Isosteric Substitutions of Urea to Thiourea and Selenourea in Aliphatic Oligourea Foldamers: Site-Specific Perturbation of the Helix Geometry
    • Nelli, Y. R.; Antunes, S.; Salaün, A.; Thinon, E.; Massip, S.; Kauffmann, B.; Douat, C.; Guichard, G. Isosteric Substitutions of Urea to Thiourea and Selenourea in Aliphatic Oligourea Foldamers: Site-Specific Perturbation of the Helix Geometry Chem.-Eur. J. 2015, 21, 2870-2880 10.1002/chem.201405792
    • (2015) Chem. - Eur. J. , vol.21 , pp. 2870-2880
    • Nelli, Y.R.1    Antunes, S.2    Salaün, A.3    Thinon, E.4    Massip, S.5    Kauffmann, B.6    Douat, C.7    Guichard, G.8
  • 46
    • 84937597214 scopus 로고    scopus 로고
    • New Class of Heterogeneous Helical Peptidomimetics
    • Wu, H.; Qiao, Q.; Teng, P.; Hu, Y.; Antoniadis, D.; Zuo, X.; Cai, J. New Class of Heterogeneous Helical Peptidomimetics Org. Lett. 2015, 17, 3524-3527 10.1021/acs.orglett.5b01608
    • (2015) Org. Lett. , vol.17 , pp. 3524-3527
    • Wu, H.1    Qiao, Q.2    Teng, P.3    Hu, Y.4    Antoniadis, D.5    Zuo, X.6    Cai, J.7
  • 47
    • 84966745503 scopus 로고    scopus 로고
    • Peptoids and Polypeptoids at the Frontier of Supra- and Macromolecular Engineering
    • Gangloff, N.; Ulbricht, J.; Lorson, T.; Schlaad, H.; Luxenhofer, R. Peptoids and Polypeptoids at the Frontier of Supra- and Macromolecular Engineering Chem. Rev. 2016, 116, 1753-1802 10.1021/acs.chemrev.5b00201
    • (2016) Chem. Rev. , vol.116 , pp. 1753-1802
    • Gangloff, N.1    Ulbricht, J.2    Lorson, T.3    Schlaad, H.4    Luxenhofer, R.5
  • 48
    • 0000908874 scopus 로고
    • Efficient Method for the Preparation of Peptoids [oligo(N-substituted glycines)] by Submonomer Solid-Phase Synthesis
    • Zuckermann, R. N.; Kerr, J. M.; Kent, S. B. H.; Moos, W. H. Efficient Method for the Preparation of Peptoids [oligo(N-substituted glycines)] by Submonomer Solid-Phase Synthesis J. Am. Chem. Soc. 1992, 114, 10646-10647 10.1021/ja00052a076
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10646-10647
    • Zuckermann, R.N.1    Kerr, J.M.2    Kent, S.B.H.3    Moos, W.H.4
  • 51
    • 84928911841 scopus 로고    scopus 로고
    • Triangular Prism-Shaped β-Peptoid Helices as Unique Biomimetic Scaffolds
    • Laursen, J. S.; Harris, P.; Fristrup, P.; Olsen, C. A. Triangular Prism-Shaped β-Peptoid Helices as Unique Biomimetic Scaffolds Nat. Commun. 2015, 6, 7013 10.1038/ncomms8013
    • (2015) Nat. Commun. , vol.6 , pp. 7013
    • Laursen, J.S.1    Harris, P.2    Fristrup, P.3    Olsen, C.A.4
  • 52
    • 77950253384 scopus 로고    scopus 로고
    • Oligooxopiperazines as Nonpeptidic α-Helix Mimetics
    • Tošovská, P.; Arora, P. S. Oligooxopiperazines as Nonpeptidic α-Helix Mimetics Org. Lett. 2010, 12, 1588-1591 10.1021/ol1003143
    • (2010) Org. Lett. , vol.12 , pp. 1588-1591
    • Tošovská, P.1    Arora, P.S.2
  • 54
    • 3543098742 scopus 로고    scopus 로고
    • Helical beta-Peptide Inhibitors of the p53-hDM2 Interaction
    • Kritzer, J. A.; Lear, J. D.; Hodsdon, M. E.; Schepartz, A. Helical beta-Peptide Inhibitors of the p53-hDM2 Interaction J. Am. Chem. Soc. 2004, 126, 9468-9469 10.1021/ja031625a
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 9468-9469
    • Kritzer, J.A.1    Lear, J.D.2    Hodsdon, M.E.3    Schepartz, A.4
  • 56
    • 33244473080 scopus 로고    scopus 로고
    • Probing the Structural Requirements of Peptoids that Inhibit HDM2-p53 Interactions
    • Hara, T.; Durell, S. R.; Myers, M. C.; Appella, D. H. Probing the Structural Requirements of Peptoids that Inhibit HDM2-p53 Interactions J. Am. Chem. Soc. 2006, 128, 1995-2004 10.1021/ja056344c
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 1995-2004
    • Hara, T.1    Durell, S.R.2    Myers, M.C.3    Appella, D.H.4
  • 57
    • 84901937652 scopus 로고    scopus 로고
    • Rational Design of Topographical Helix Mimics as Potent Inhibitors of Protein-Protein Interactions
    • Lao, B. B.; Drew, K.; Guarracino, D. A.; Brewer, T. F.; Heindel, D. W.; Bonneau, R.; Arora, P. S. Rational Design of Topographical Helix Mimics as Potent Inhibitors of Protein-Protein Interactions J. Am. Chem. Soc. 2014, 136, 7877-7888 10.1021/ja502310r
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 7877-7888
    • Lao, B.B.1    Drew, K.2    Guarracino, D.A.3    Brewer, T.F.4    Heindel, D.W.5    Bonneau, R.6    Arora, P.S.7
  • 58
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 Protein Family: Arbiters of Cell Survival
    • Adams, J. M.; Cory, S. The Bcl-2 Protein Family: Arbiters of Cell Survival Science 1998, 281, 1322-1326 10.1126/science.281.5381.1322
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 59
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 Domains Either Sensitize or Activate Mitochondrial Apoptosis, Serving as Prototype Cancer Therapeutics
    • Letai, A.; Bassik, M. C.; Walensky, L. D.; Sorcinelli, M. D.; Weiler, S.; Korsmeyer, S. J. Distinct BH3 Domains Either Sensitize or Activate Mitochondrial Apoptosis, Serving as Prototype Cancer Therapeutics Cancer Cell 2002, 2, 183-192 10.1016/S1535-6108(02)00127-7
    • (2002) Cancer Cell , vol.2 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 60
    • 24144488383 scopus 로고    scopus 로고
    • Chimeric (α/β + α)-Peptide Ligands for the BH3-Recognition Cleft of Bcl-xL: Critical Role of the Molecular Scaffold in Protein Surface Recognition
    • Sadowsky, J. D.; Schmitt, M. A.; Lee, H.-S.; Umezawa, N.; Wang, S.; Tomita, Y.; Gellman, S. H. Chimeric (α/β + α)-Peptide Ligands for the BH3-Recognition Cleft of Bcl-xL: Critical Role of the Molecular Scaffold in Protein Surface Recognition J. Am. Chem. Soc. 2005, 127, 11966-11968 10.1021/ja053678t
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 11966-11968
    • Sadowsky, J.D.1    Schmitt, M.A.2    Lee, H.-S.3    Umezawa, N.4    Wang, S.5    Tomita, Y.6    Gellman, S.H.7
  • 62
    • 46449115491 scopus 로고    scopus 로고
    • Hydrophile Scanning as a Complement to Alanine Scanning for Exploring and Manipulating Protein-Protein Recognition: Application to the Bim BH3 Domain
    • Boersma, M. D.; Sadowsky, J. D.; Tomita, Y. A.; Gellman, S. H. Hydrophile Scanning as a Complement to Alanine Scanning for Exploring and Manipulating Protein-Protein Recognition: Application to the Bim BH3 Domain Protein Sci. 2008, 17, 1232-1240 10.1110/ps.032896.107
    • (2008) Protein Sci. , vol.17 , pp. 1232-1240
    • Boersma, M.D.1    Sadowsky, J.D.2    Tomita, Y.A.3    Gellman, S.H.4
  • 63
    • 34447558127 scopus 로고    scopus 로고
    • Exploration of Backbone Space in Foldamers Containing α- And β-Amino Acid Residues: Developing Protease-Resistant Oligomers that Bind Tightly to the BH3-Recognition Cleft of Bcl-xL
    • Sadowsky, J. D.; Murray, J. K.; Tomita, Y.; Gellman, S. H. Exploration of Backbone Space in Foldamers Containing α- and β-Amino Acid Residues: Developing Protease-Resistant Oligomers that Bind Tightly to the BH3-Recognition Cleft of Bcl-xL ChemBioChem 2007, 8, 903-916 10.1002/cbic.200600546
    • (2007) ChemBioChem , vol.8 , pp. 903-916
    • Sadowsky, J.D.1    Murray, J.K.2    Tomita, Y.3    Gellman, S.H.4
  • 64
    • 42249109845 scopus 로고    scopus 로고
    • Sequence-Based Design of alpha/beta-Peptide Foldamers that Mimic BH3 Domains
    • Horne, W. S.; Boersma, M. D.; Windsor, M. A.; Gellman, S. H. Sequence-Based Design of alpha/beta-Peptide Foldamers that Mimic BH3 Domains Angew. Chem., Int. Ed. 2008, 47, 2853-2856 10.1002/anie.200705315
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 2853-2856
    • Horne, W.S.1    Boersma, M.D.2    Windsor, M.A.3    Gellman, S.H.4
  • 65
    • 80052175637 scopus 로고    scopus 로고
    • Structural Basis of Bcl-xL Recognition by a BH3-Mimetic α/β-peptide Generated by Sequence-Based Design
    • Lee, E. F.; Smith, B. J.; Horne, W. S.; Mayer, K. N.; Evangelista, M.; Colman, P. M.; Gellman, S. H.; Fairlie, W. D. Structural Basis of Bcl-xL Recognition by a BH3-Mimetic α/β-peptide Generated by Sequence-Based Design ChemBioChem 2011, 12, 2025-2032 10.1002/cbic.201100314
    • (2011) ChemBioChem , vol.12 , pp. 2025-2032
    • Lee, E.F.1    Smith, B.J.2    Horne, W.S.3    Mayer, K.N.4    Evangelista, M.5    Colman, P.M.6    Gellman, S.H.7    Fairlie, W.D.8
  • 66
    • 84883165577 scopus 로고    scopus 로고
    • Structure-Guided Rational Design of α/β-peptide Foldamers with High Affinity for BCL-2 Family Prosurvival Proteins
    • Smith, B. J.; Lee, E. F.; Checco, J. W.; Evangelista, M.; Gellman, S. H.; Fairlie, W. D. Structure-Guided Rational Design of α/β-peptide Foldamers with High Affinity for BCL-2 Family Prosurvival Proteins ChemBioChem 2013, 14, 1564-1572 10.1002/cbic.201300351
    • (2013) ChemBioChem , vol.14 , pp. 1564-1572
    • Smith, B.J.1    Lee, E.F.2    Checco, J.W.3    Evangelista, M.4    Gellman, S.H.5    Fairlie, W.D.6
  • 68
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
    • Kussie, P. H.; Gorina, S.; Marechal, V.; Elenbaas, B.; Moreau, J.; Levine, A. J.; Pavletich, N. P. Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain Science 1996, 274, 948-953 10.1126/science.274.5289.948
    • (1996) Science , vol.274 , pp. 948-953
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3    Elenbaas, B.4    Moreau, J.5    Levine, A.J.6    Pavletich, N.P.7
  • 69
    • 0030604722 scopus 로고    scopus 로고
    • Crystal Structures of a Complexed and Peptide-Free Membrane Protein-Binding Domain: Molecular Basis of Peptide Recognition by PDZ
    • Doyle, D. A.; Lee, A.; Lewis, J.; Kim, E.; Sheng, M.; MacKinnon, R. Crystal Structures of a Complexed and Peptide-Free Membrane Protein-Binding Domain: Molecular Basis of Peptide Recognition by PDZ Cell 1996, 85, 1067-1076 10.1016/S0092-8674(00)81307-0
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    MacKinnon, R.6
  • 75
    • 84860390239 scopus 로고    scopus 로고
    • An Orthosteric Inhibitor of the Ras-Sos Interaction
    • Patgiri, A.; Yadav, K. K.; Arora, P. S.; Bar-Sagi, D. An Orthosteric Inhibitor of the Ras-Sos Interaction Nat. Chem. Biol. 2011, 7, 585-587 10.1038/nchembio.612
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 585-587
    • Patgiri, A.1    Yadav, K.K.2    Arora, P.S.3    Bar-Sagi, D.4
  • 77
    • 31044441154 scopus 로고    scopus 로고
    • Structure and Function of the Platelet Integrin alphaIIbbeta3
    • Bennett, J. S. Structure and Function of the Platelet Integrin alphaIIbbeta3 J. Clin. Invest. 2005, 115, 3363-3369 10.1172/JCI26989
    • (2005) J. Clin. Invest. , vol.115 , pp. 3363-3369
    • Bennett, J.S.1
  • 80
    • 77954059555 scopus 로고    scopus 로고
    • Crystal Structure of HIV-1 gp41 Including Both Fusion Peptide and Membrane Proximal External Regions
    • Buzon, V.; Natrajan, G.; Schibli, D.; Campelo, F.; Kozlov, M. M.; Weissenhorn, W. Crystal Structure of HIV-1 gp41 Including Both Fusion Peptide and Membrane Proximal External Regions PLoS Pathog. 2010, 6, e1000880 10.1371/journal.ppat.1000880
    • (2010) PLoS Pathog. , vol.6 , pp. e1000880
    • Buzon, V.1    Natrajan, G.2    Schibli, D.3    Campelo, F.4    Kozlov, M.M.5    Weissenhorn, W.6
  • 83
    • 79959861233 scopus 로고    scopus 로고
    • Broad Distribution of Energetically Important Contacts across an Extended Protein Interface
    • Johnson, L. M.; Horne, W. S.; Gellman, S. H. Broad Distribution of Energetically Important Contacts across an Extended Protein Interface J. Am. Chem. Soc. 2011, 133, 10038-10041 10.1021/ja203358t
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 10038-10041
    • Johnson, L.M.1    Horne, W.S.2    Gellman, S.H.3
  • 84
    • 84860799886 scopus 로고    scopus 로고
    • Enhancement of α-helix Mimicry by an α/β-Peptide Foldamer via Incorporation of a Dense Ionic Side-Chain Array
    • Johnson, L. M.; Mortenson, D. E.; Yun, H. G.; Horne, W. S.; Ketas, T. J.; Lu, M.; Moore, J. P.; Gellman, S. H. Enhancement of α-helix Mimicry by an α/β-Peptide Foldamer via Incorporation of a Dense Ionic Side-Chain Array J. Am. Chem. Soc. 2012, 134, 7317-7320 10.1021/ja302428d
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 7317-7320
    • Johnson, L.M.1    Mortenson, D.E.2    Yun, H.G.3    Horne, W.S.4    Ketas, T.J.5    Lu, M.6    Moore, J.P.7    Gellman, S.H.8
  • 85
    • 33646357930 scopus 로고    scopus 로고
    • Rational Development of beta-Peptide Inhibitors of Human Cytomegalovirus Entry
    • English, E. P.; Chumanov, R. S.; Gellman, S. H.; Compton, T. Rational Development of beta-Peptide Inhibitors of Human Cytomegalovirus Entry J. Biol. Chem. 2006, 281, 2661-2667 10.1074/jbc.M508485200
    • (2006) J. Biol. Chem. , vol.281 , pp. 2661-2667
    • English, E.P.1    Chumanov, R.S.2    Gellman, S.H.3    Compton, T.4
  • 86
    • 42449160533 scopus 로고    scopus 로고
    • Molecular Recognition of Parathyroid Hormone by its G Protein-Coupled Receptor
    • Pioszak, A. A.; Xu, H. E. Molecular Recognition of Parathyroid Hormone by its G Protein-Coupled Receptor Proc. Natl. Acad. Sci. U. S. A. 2008, 105, 5034-5039 10.1073/pnas.0801027105
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 5034-5039
    • Pioszak, A.A.1    Xu, H.E.2
  • 87
    • 84903964236 scopus 로고    scopus 로고
    • Backbone Modification of a Polypeptide Drug Alters Duration of Action in vivo
    • Cheloha, R. W.; Maeda, A.; Dean, T.; Gardella, T. J.; Gellman, S. H. Backbone Modification of a Polypeptide Drug Alters Duration of Action in vivo Nat. Biotechnol. 2014, 32, 653-655 10.1038/nbt.2920
    • (2014) Nat. Biotechnol. , vol.32 , pp. 653-655
    • Cheloha, R.W.1    Maeda, A.2    Dean, T.3    Gardella, T.J.4    Gellman, S.H.5
  • 88
    • 73649107900 scopus 로고    scopus 로고
    • Crystal Structure of Glucagon-like Peptide-1 in Complex with the Extracellular Domain of the Glucagon-like Peptide-1 Receptor
    • Underwood, C. R.; Garibay, P.; Knudsen, L. B.; Hastrup, S.; Peters, G. H.; Rudolph, R.; Reedtz-Runge, S. Crystal Structure of Glucagon-like Peptide-1 in Complex with the Extracellular Domain of the Glucagon-like Peptide-1 Receptor J. Biol. Chem. 2010, 285, 723-730 10.1074/jbc.M109.033829
    • (2010) J. Biol. Chem. , vol.285 , pp. 723-730
    • Underwood, C.R.1    Garibay, P.2    Knudsen, L.B.3    Hastrup, S.4    Peters, G.H.5    Rudolph, R.6    Reedtz-Runge, S.7
  • 90
    • 84870054636 scopus 로고    scopus 로고
    • GLP-1 Receptor Agonists for Individualized Treatment of Type 2 Diabetes Mellitus
    • Meier, J. J. GLP-1 Receptor Agonists for Individualized Treatment of Type 2 Diabetes Mellitus Nat. Rev. Endocrinol. 2012, 8, 728-742 10.1038/nrendo.2012.140
    • (2012) Nat. Rev. Endocrinol. , vol.8 , pp. 728-742
    • Meier, J.J.1
  • 91
    • 84922790807 scopus 로고    scopus 로고
    • GLP-1 Receptor Agonists: A Review of Head-to-Head Clinical Studies
    • Trujillo, J. M.; Nuffer, W.; Ellis, S. L. GLP-1 Receptor Agonists: A Review of Head-to-Head Clinical Studies Ther. Adv. Endocrinol. Metab. 2015, 6, 19-28 10.1177/2042018814559725
    • (2015) Ther. Adv. Endocrinol. Metab. , vol.6 , pp. 19-28
    • Trujillo, J.M.1    Nuffer, W.2    Ellis, S.L.3
  • 92
    • 24944436267 scopus 로고    scopus 로고
    • Neutral Endopeptidase 24.11 and Dipeptidyl Peptidase IV are Both Mediators of the Degradation of Glucagon-like Peptide 1 in the Anaesthetised Pig
    • Plamboeck, A.; Holst, J. J.; Carr, R. D.; Deacon, C. F. Neutral Endopeptidase 24.11 and Dipeptidyl Peptidase IV are Both Mediators of the Degradation of Glucagon-like Peptide 1 in the Anaesthetised Pig Diabetologia 2005, 48, 1882-1890 10.1007/s00125-005-1847-7
    • (2005) Diabetologia , vol.48 , pp. 1882-1890
    • Plamboeck, A.1    Holst, J.J.2    Carr, R.D.3    Deacon, C.F.4
  • 93
    • 0032908654 scopus 로고    scopus 로고
    • Glucose-Lowering and Insulin-Sensitizing Actions of Exendin-4 - Studies in Obese Diabetic (ob/ob, db/db) Mice, Diabetic Fatty Zucker Rats, and Diabetic Rhesus Monkeys (Macaca mulatta)
    • Young, A. A.; Gedulin, B. R.; Bhavsar, S.; Bodkin, N.; Jodka, C.; Hansen, B.; Denaro, M. Glucose-Lowering and Insulin-Sensitizing Actions of Exendin-4-Studies in Obese Diabetic (ob/ob, db/db) Mice, Diabetic Fatty Zucker Rats, and Diabetic Rhesus Monkeys (Macaca mulatta) Diabetes 1999, 48, 1026-1034 10.2337/diabetes.48.5.1026
    • (1999) Diabetes , vol.48 , pp. 1026-1034
    • Young, A.A.1    Gedulin, B.R.2    Bhavsar, S.3    Bodkin, N.4    Jodka, C.5    Hansen, B.6    Denaro, M.7
  • 94
    • 0035913057 scopus 로고    scopus 로고
    • Peptide Folding Induces High and Selective Affinity of a Linear and Small beta-Peptide to the Human Somatostatin Receptor 4
    • Gademann, K.; Kimmerlin, T.; Hoyer, D.; Seebach, D. Peptide Folding Induces High and Selective Affinity of a Linear and Small beta-Peptide to the Human Somatostatin Receptor 4 J. Med. Chem. 2001, 44, 2460-2468 10.1021/jm010816q
    • (2001) J. Med. Chem. , vol.44 , pp. 2460-2468
    • Gademann, K.1    Kimmerlin, T.2    Hoyer, D.3    Seebach, D.4
  • 96
    • 34248333311 scopus 로고    scopus 로고
    • Therapeutical Approaches of Vasoactive Intestinal Peptide as a Pleiotropic Immunomodulator
    • Gonzalez-Rey, E.; Varela, N.; Chorny, A.; Delgado, M. Therapeutical Approaches of Vasoactive Intestinal Peptide as a Pleiotropic Immunomodulator Curr. Pharm. Des. 2007, 13, 1113-1139 10.2174/138161207780618966
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 1113-1139
    • Gonzalez-Rey, E.1    Varela, N.2    Chorny, A.3    Delgado, M.4
  • 97
    • 0028032460 scopus 로고
    • Two Receptors for Vasoactive Intestinal Polypeptide with Similar Specificity and Complementary Distributions
    • Usdin, T. B.; Bonner, T. I.; Mezey, E. Two Receptors for Vasoactive Intestinal Polypeptide with Similar Specificity and Complementary Distributions Endocrinology 1994, 135, 2662-2680 10.1210/endo.135.6.7988457
    • (1994) Endocrinology , vol.135 , pp. 2662-2680
    • Usdin, T.B.1    Bonner, T.I.2    Mezey, E.3
  • 100
    • 33845499030 scopus 로고    scopus 로고
    • Beta Strand Peptidomimetics as Potent PDZ Domain Ligands
    • Hammond, M. C.; Harris, B. Z.; Lim, W. A.; Bartlett, P. A. Beta Strand Peptidomimetics as Potent PDZ Domain Ligands Chem. Biol. 2006, 13, 1247-1251 10.1016/j.chembiol.2006.11.010
    • (2006) Chem. Biol. , vol.13 , pp. 1247-1251
    • Hammond, M.C.1    Harris, B.Z.2    Lim, W.A.3    Bartlett, P.A.4
  • 101
    • 5044224260 scopus 로고    scopus 로고
    • PDZ Domain Proteins of Synapses
    • Kim, E.; Sheng, M. PDZ Domain Proteins of Synapses Nat. Rev. Neurosci. 2004, 5, 771-781 10.1038/nrn1517
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 771-781
    • Kim, E.1    Sheng, M.2
  • 102
    • 15744402961 scopus 로고    scopus 로고
    • Effects of Conformational Stability and Geometry of Guanidinium Display on Cell Entry by β-Peptides
    • Potocky, T. B.; Menon, A. K.; Gellman, S. H. Effects of Conformational Stability and Geometry of Guanidinium Display on Cell Entry by β-Peptides J. Am. Chem. Soc. 2005, 127, 3686-3687 10.1021/ja042566j
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 3686-3687
    • Potocky, T.B.1    Menon, A.K.2    Gellman, S.H.3
  • 103
    • 84929352950 scopus 로고    scopus 로고
    • A Preorganized β-Amino Acid Bearing a Guanidinium Side Chain and its use in Cell-Penetrating Peptides
    • Demizu, Y.; Oba, M.; Okitsu, K.; Yamashita, H.; Misawa, T.; Tanaka, M.; Kurihara, M.; Gellman, S. H. A Preorganized β-Amino Acid Bearing a Guanidinium Side Chain and its use in Cell-Penetrating Peptides Org. Biomol. Chem. 2015, 13, 5617-5620 10.1039/C5OB00389J
    • (2015) Org. Biomol. Chem. , vol.13 , pp. 5617-5620
    • Demizu, Y.1    Oba, M.2    Okitsu, K.3    Yamashita, H.4    Misawa, T.5    Tanaka, M.6    Kurihara, M.7    Gellman, S.H.8
  • 105
    • 13744249482 scopus 로고    scopus 로고
    • DOTAP (and other Cationic Lipids): Chemistry, Biophysics and Transfection
    • Simberg, D.; Weisman, S.; Talmon, Y.; Barenholz, Y. DOTAP (and other Cationic Lipids): Chemistry, Biophysics and Transfection Crit. Rev. Ther. Drug Carrier Syst. 2004, 21, 257-317 10.1615/CritRevTherDrugCarrierSyst.v21.i4.10
    • (2004) Crit. Rev. Ther. Drug Carrier Syst. , vol.21 , pp. 257-317
    • Simberg, D.1    Weisman, S.2    Talmon, Y.3    Barenholz, Y.4
  • 106
    • 84927176453 scopus 로고    scopus 로고
    • A Review of the Developments of Characteristics of PEI derivatives for Gene Delivery Applications
    • Taranejoo, S.; Liu, J.; Verma, P.; Hourigan, K. A Review of the Developments of Characteristics of PEI derivatives for Gene Delivery Applications J. Appl. Polym. Sci. 2015, 132, 42096 10.1002/app.42096
    • (2015) J. Appl. Polym. Sci. , vol.132 , pp. 42096
    • Taranejoo, S.1    Liu, J.2    Verma, P.3    Hourigan, K.4
  • 107
    • 0036469507 scopus 로고    scopus 로고
    • Heparin-Protein Interactions
    • Capila, I.; Linhardt, R. J. Heparin-Protein Interactions Angew. Chem., Int. Ed. 2002, 41, 390-412 10.1002/1521-3773(20020201)41:3<390::AID-ANIE390>3.0.CO;2-B
    • (2002) Angew. Chem., Int. Ed. , vol.41 , pp. 390-412
    • Capila, I.1    Linhardt, R.J.2
  • 108
    • 0022468247 scopus 로고
    • A Comparison of the Strength of Binding of Antithrombin III, Protamine and Poly(L-lysine) to Heparin Samples of Different Anticoagulant Activities
    • Jones, G. R.; Hashim, R.; Power, D. M. A Comparison of the Strength of Binding of Antithrombin III, Protamine and Poly(L-lysine) to Heparin Samples of Different Anticoagulant Activities Biochim. Biophys. Acta, Gen. Subj. 1986, 883, 69-76 10.1016/0304-4165(86)90136-4
    • (1986) Biochim. Biophys. Acta, Gen. Subj. , vol.883 , pp. 69-76
    • Jones, G.R.1    Hashim, R.2    Power, D.M.3
  • 109
    • 33845461883 scopus 로고    scopus 로고
    • Low Molecular Weight Protamine as Nontoxic Heparin/Low Molecular Weight Heparin Antidote (III): Preliminary in vivo Evaluation of Efficacy and Toxicity Using a Canine Model
    • Lee, L. M.; Chang, L. C.; Wrobleski, S.; Wakefield, T. W.; Yang, V. C. Low Molecular Weight Protamine as Nontoxic Heparin/Low Molecular Weight Heparin Antidote (III): Preliminary in vivo Evaluation of Efficacy and Toxicity Using a Canine Model AAPS PharmSci. 2001, 3, E19
    • (2001) AAPS PharmSci. , vol.3 , pp. E19
    • Lee, L.M.1    Chang, L.C.2    Wrobleski, S.3    Wakefield, T.W.4    Yang, V.C.5
  • 112
    • 34247884335 scopus 로고    scopus 로고
    • Macrocyclic β-Sheet Peptides That Mimic Protein Quaternary Structure through Intermolecular β-Sheet Interactions
    • Khakshoor, O.; Demeler, B.; Nowick, J. S. Macrocyclic β-Sheet Peptides That Mimic Protein Quaternary Structure through Intermolecular β-Sheet Interactions J. Am. Chem. Soc. 2007, 129, 5558-5569 10.1021/ja068511u
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5558-5569
    • Khakshoor, O.1    Demeler, B.2    Nowick, J.S.3
  • 113
    • 67949112621 scopus 로고    scopus 로고
    • Alkyne-Linked 2,2-Disubstituted-indolin-3-one Oligomers as Extended β-Strand Mimetics
    • Wyrembak, P. N.; Hamilton, A. D. Alkyne-Linked 2,2-Disubstituted-indolin-3-one Oligomers as Extended β-Strand Mimetics J. Am. Chem. Soc. 2009, 131, 4566-4567 10.1021/ja809245t
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 4566-4567
    • Wyrembak, P.N.1    Hamilton, A.D.2
  • 114
    • 0041520533 scopus 로고    scopus 로고
    • Duplex Foldamers from Assembly Induced Folding
    • Yang, X.; Martinovic, S.; Smith, R. D.; Gong, B. Duplex Foldamers from Assembly Induced Folding J. Am. Chem. Soc. 2003, 125, 9932-9933 10.1021/ja0361897
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9932-9933
    • Yang, X.1    Martinovic, S.2    Smith, R.D.3    Gong, B.4
  • 115
    • 84878325210 scopus 로고    scopus 로고
    • Design, Synthesis, and Characterization of Heparin-Binding Peptoids
    • Ford, B. K.; Hamza, M.; Rabenstein, D. L. Design, Synthesis, and Characterization of Heparin-Binding Peptoids Biochemistry 2013, 52, 3773-3780 10.1021/bi4001722
    • (2013) Biochemistry , vol.52 , pp. 3773-3780
    • Ford, B.K.1    Hamza, M.2    Rabenstein, D.L.3
  • 116
    • 17344384874 scopus 로고    scopus 로고
    • Antibitoics: Non-Haemolytic β-Amino-Acid Oligomers
    • Porter, E. A.; Wang, X.; Lee, H.; Weisblum, B.; Gellman, S. H. Antibitoics: Non-Haemolytic β-Amino-Acid Oligomers Nature 2000, 404, 565 10.1038/35007145
    • (2000) Nature , vol.404 , pp. 565
    • Porter, E.A.1    Wang, X.2    Lee, H.3    Weisblum, B.4    Gellman, S.H.5
  • 117
    • 0033616105 scopus 로고    scopus 로고
    • De Novo Design of Antibacterial β-peptides
    • Hamuro, Y.; Schneider, J. P.; DeGrado, W. F. De Novo Design of Antibacterial β-peptides J. Am. Chem. Soc. 1999, 121, 12200-12201 10.1021/ja992728p
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 12200-12201
    • Hamuro, Y.1    Schneider, J.P.2    DeGrado, W.F.3
  • 118
    • 84908140613 scopus 로고    scopus 로고
    • Synthetic Polymers Active against Clostridium difficile Vegetative Cell Growth and Spore Outgrowth
    • Liu, R.; Suarez, J. M.; Weisblum, B.; Gellman, S. H.; McBride, S. M. Synthetic Polymers Active against Clostridium difficile Vegetative Cell Growth and Spore Outgrowth J. Am. Chem. Soc. 2014, 136, 14498-14504 10.1021/ja506798e
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 14498-14504
    • Liu, R.1    Suarez, J.M.2    Weisblum, B.3    Gellman, S.H.4    McBride, S.M.5
  • 119
    • 0014381393 scopus 로고
    • Conformation of Polypeptides and Proteins
    • Ramachandran, G. N.; Sasisekharan, V. Conformation of Polypeptides and Proteins Adv. Protein Chem. 1968, 23, 283-438 10.1016/S0065-3233(08)60402-7
    • (1968) Adv. Protein Chem. , vol.23 , pp. 283-438
    • Ramachandran, G.N.1    Sasisekharan, V.2
  • 120
    • 34047181039 scopus 로고    scopus 로고
    • Design and Synthesis of Chiral Alpha,Alpha-Disubstituted Amino Acids and Conformational Study of their Oligopeptides
    • Tanaka, M. Design and Synthesis of Chiral Alpha,Alpha-Disubstituted Amino Acids and Conformational Study of their Oligopeptides Chem. Pharm. Bull. 2007, 55, 349-358 10.1248/cpb.55.349
    • (2007) Chem. Pharm. Bull. , vol.55 , pp. 349-358
    • Tanaka, M.1
  • 121
    • 52149116532 scopus 로고    scopus 로고
    • Aib Residues in Peptaibiotics and Synthetic Sequences: Analysis of Nonhelical Conformations
    • Aravinda, S.; Shamala, N.; Balaram, P. Aib Residues in Peptaibiotics and Synthetic Sequences: Analysis of Nonhelical Conformations Chem. Biodiversity 2008, 5, 1238-1262 10.1002/cbdv.200890112
    • (2008) Chem. Biodiversity , vol.5 , pp. 1238-1262
    • Aravinda, S.1    Shamala, N.2    Balaram, P.3
  • 122
    • 84939615651 scopus 로고    scopus 로고
    • Peptide Backbone Composition and Protease Susceptibility: Impact of Modification Type, Position, and Tandem Substitution
    • Werner, H. M.; Cabalteja, C. C.; Horne, W. S. Peptide Backbone Composition and Protease Susceptibility: Impact of Modification Type, Position, and Tandem Substitution ChemBioChem 2016, 17, 712-718 10.1002/cbic.201500312
    • (2016) ChemBioChem , vol.17 , pp. 712-718
    • Werner, H.M.1    Cabalteja, C.C.2    Horne, W.S.3
  • 123
    • 34447322795 scopus 로고    scopus 로고
    • The History of Alamethicin: A Review of the Most Extensively Studied Peptaibol
    • Leitgeb, B.; Szekeres, A.; Manczinger, L.; Vágvölgyi, C.; Kredics, L. The History of Alamethicin: A Review of the Most Extensively Studied Peptaibol Chem. Biodiversity 2007, 4, 1027-1051 10.1002/cbdv.200790095
    • (2007) Chem. Biodiversity , vol.4 , pp. 1027-1051
    • Leitgeb, B.1    Szekeres, A.2    Manczinger, L.3    Vágvölgyi, C.4    Kredics, L.5
  • 125
    • 0034867234 scopus 로고    scopus 로고
    • Peptaibols: Models for Ion Channels
    • Chugh, J. K.; Wallace, B. A. Peptaibols: Models for Ion Channels Biochem. Soc. Trans. 2001, 29, 565-570 10.1042/bst0290565
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 565-570
    • Chugh, J.K.1    Wallace, B.A.2
  • 126
    • 0029821111 scopus 로고    scopus 로고
    • Antimicrobial α,α-Dialkylated Amino Acid Rich Peptides with in-Vivo Activity Against an Intracellular Pathogen
    • Yokum, T. S.; Elzer, P. H.; McLaughlin, M. L. Antimicrobial α,α-Dialkylated Amino Acid Rich Peptides with in-Vivo Activity Against an Intracellular Pathogen J. Med. Chem. 1996, 39, 3603-3605 10.1021/jm960451n
    • (1996) J. Med. Chem. , vol.39 , pp. 3603-3605
    • Yokum, T.S.1    Elzer, P.H.2    McLaughlin, M.L.3
  • 133
    • 12344251969 scopus 로고    scopus 로고
    • Simple, Helical Peptoid Analogs of Lung Surfactant Protein B
    • Seurynck, S. L.; Patch, J. A.; Barron, A. E. Simple, Helical Peptoid Analogs of Lung Surfactant Protein B Chem. Biol. 2005, 12, 77-88 10.1016/j.chembiol.2004.10.014
    • (2005) Chem. Biol. , vol.12 , pp. 77-88
    • Seurynck, S.L.1    Patch, J.A.2    Barron, A.E.3
  • 134
    • 0344928208 scopus 로고    scopus 로고
    • Helical Peptoid Mimics of Lung Surfactant Protein C
    • Wu, C. W.; Seurynck, S. L.; Lee, K. Y. C.; Barron, A. E. Helical Peptoid Mimics of Lung Surfactant Protein C Chem. Biol. 2003, 10, 1057-1063 10.1016/j.chembiol.2003.10.008
    • (2003) Chem. Biol. , vol.10 , pp. 1057-1063
    • Wu, C.W.1    Seurynck, S.L.2    Lee, K.Y.C.3    Barron, A.E.4
  • 135
    • 80053485066 scopus 로고    scopus 로고
    • Peptoids: Bio-Inspired Polymers as Potential Pharmaceuticals
    • Dohm, M. T.; Kapoor, R.; Barron, A. E. Peptoids: Bio-Inspired Polymers as Potential Pharmaceuticals Curr. Pharm. Des. 2011, 17, 2732-2747 10.2174/138161211797416066
    • (2011) Curr. Pharm. Des. , vol.17 , pp. 2732-2747
    • Dohm, M.T.1    Kapoor, R.2    Barron, A.E.3
  • 136
  • 137
    • 0032881267 scopus 로고    scopus 로고
    • β-Peptides as Inhibitors of Small-Intestinal Cholesterol and Fat Absorption
    • Werder, M.; Hauser, H.; Abele, S.; Seebach, D. β-Peptides as Inhibitors of Small-Intestinal Cholesterol and Fat Absorption Helv. Chim. Acta 1999, 82, 1774-1783 10.1002/(SICI)1522-2675(19991006)82:10<1774::AID-HLCA1774>3.0.CO;2-O
    • (1999) Helv. Chim. Acta , vol.82 , pp. 1774-1783
    • Werder, M.1    Hauser, H.2    Abele, S.3    Seebach, D.4
  • 138
    • 0032133429 scopus 로고    scopus 로고
    • Peptidomimetic Design
    • Ripka, A. S.; Rich, D. H. Peptidomimetic Design Curr. Opin. Chem. Biol. 1998, 2, 441-452 10.1016/S1367-5931(98)80119-1
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 441-452
    • Ripka, A.S.1    Rich, D.H.2
  • 139
    • 33748216403 scopus 로고
    • Novel Molecular Scaffolds: Formation of Helical Secondary Structure in a Family of Oligoanthranilamides
    • Hamuro, Y.; Geib, S. J.; Hamilton, A. D. Novel Molecular Scaffolds: Formation of Helical Secondary Structure in a Family of Oligoanthranilamides Angew. Chem., Int. Ed. Engl. 1994, 33, 446-448 10.1002/anie.199404461
    • (1994) Angew. Chem., Int. Ed. Engl. , vol.33 , pp. 446-448
    • Hamuro, Y.1    Geib, S.J.2    Hamilton, A.D.3
  • 140
    • 0029759396 scopus 로고    scopus 로고
    • Oligoanthranilamides. Non-Peptide Subunits That Show Formation of Specific Secondary Structure
    • Hamuro, Y.; Geib, S. J.; Hamilton, A. D. Oligoanthranilamides. Non-Peptide Subunits That Show Formation of Specific Secondary Structure J. Am. Chem. Soc. 1996, 118, 7529-7541 10.1021/ja9539857
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7529-7541
    • Hamuro, Y.1    Geib, S.J.2    Hamilton, A.D.3
  • 141
    • 0034801374 scopus 로고    scopus 로고
    • Toward Proteomimetics: Terphenyl Derivatives as Structural and Functional Mimics of Extended Regions of an α-Helix
    • Orner, B. P.; Ernst, J. T.; Hamilton, A. D. Toward Proteomimetics: Terphenyl Derivatives as Structural and Functional Mimics of Extended Regions of an α-Helix J. Am. Chem. Soc. 2001, 123, 5382-5383 10.1021/ja0025548
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5382-5383
    • Orner, B.P.1    Ernst, J.T.2    Hamilton, A.D.3
  • 142
    • 4644337027 scopus 로고    scopus 로고
    • Hydrogen-Bonding-Induced Planar, Rigid, and Zigzag Oligoanthranilamides. Synthesis, Characterization, and Self-Assembly of a Metallocyclophane
    • Zhu, J.; Wang, X.-Z.; Chen, Y.-Q.; Jiang, X.-K.; Chen, X.-Z.; Li, Z.-T. Hydrogen-Bonding-Induced Planar, Rigid, and Zigzag Oligoanthranilamides. Synthesis, Characterization, and Self-Assembly of a Metallocyclophane J. Org. Chem. 2004, 69, 6221-6227 10.1021/jo0490705
    • (2004) J. Org. Chem. , vol.69 , pp. 6221-6227
    • Zhu, J.1    Wang, X.-Z.2    Chen, Y.-Q.3    Jiang, X.-K.4    Chen, X.-Z.5    Li, Z.-T.6
  • 143
    • 0037415861 scopus 로고    scopus 로고
    • Design and Application of an α-Helix-Mimetic Scaffold Based on an Oligoamide-Foldamer Strategy: Antagonism of the Bak BH3/Bcl-xL Complex
    • Ernst, J. T.; Becerril, J.; Park, H. S.; Yin, H.; Hamilton, A. D. Design and Application of an α-Helix-Mimetic Scaffold Based on an Oligoamide-Foldamer Strategy: Antagonism of the Bak BH3/Bcl-xL Complex Angew. Chem., Int. Ed. 2003, 42, 535-539 10.1002/anie.200390154
    • (2003) Angew. Chem., Int. Ed. , vol.42 , pp. 535-539
    • Ernst, J.T.1    Becerril, J.2    Park, H.S.3    Yin, H.4    Hamilton, A.D.5
  • 145
    • 33748438219 scopus 로고    scopus 로고
    • Intramolecular Hydrogen Bonding Allows Simple Enaminones to Structurally Mimic the i, i + 4, and i + 7 Residues of an α-Helix
    • Rodriguez, J. M.; Hamilton, A. D. Intramolecular Hydrogen Bonding Allows Simple Enaminones to Structurally Mimic the i, i + 4, and i + 7 Residues of an α-Helix Tetrahedron Lett. 2006, 47, 7443-7446 10.1016/j.tetlet.2006.08.048
    • (2006) Tetrahedron Lett. , vol.47 , pp. 7443-7446
    • Rodriguez, J.M.1    Hamilton, A.D.2
  • 146
    • 34247138372 scopus 로고    scopus 로고
    • Facile Synthesis of Benzamides to Mimic an α-Helix
    • Ahn, J.-M.; Han, S.-Y. Facile Synthesis of Benzamides to Mimic an α-Helix Tetrahedron Lett. 2007, 48, 3543-3547 10.1016/j.tetlet.2007.03.108
    • (2007) Tetrahedron Lett. , vol.48 , pp. 3543-3547
    • Ahn, J.-M.1    Han, S.-Y.2
  • 147
    • 0034641910 scopus 로고    scopus 로고
    • Interconversion of Single and Double Helices Formed from Synthetic Molecular Strands
    • Berl, V.; Huc, I.; Khoury, R. G.; Krische, M. J.; Lehn, J.-M. Interconversion of Single and Double Helices Formed from Synthetic Molecular Strands Nature 2000, 407, 720-723 10.1038/35037545
    • (2000) Nature , vol.407 , pp. 720-723
    • Berl, V.1    Huc, I.2    Khoury, R.G.3    Krische, M.J.4    Lehn, J.-M.5
  • 148
    • 0037715341 scopus 로고    scopus 로고
    • Protonation-Induced Transition between Two Distinct Helical Conformations of a Synthetic Oligomer via a Linear Intermediate
    • Dolain, C.; Maurizot, V.; Huc, I. Protonation-Induced Transition between Two Distinct Helical Conformations of a Synthetic Oligomer via a Linear Intermediate Angew. Chem., Int. Ed. 2003, 42, 2738-2740 10.1002/anie.200351080
    • (2003) Angew. Chem., Int. Ed. , vol.42 , pp. 2738-2740
    • Dolain, C.1    Maurizot, V.2    Huc, I.3
  • 150
    • 0035980345 scopus 로고    scopus 로고
    • Complexation-Induced Unfolding of Heterocyclic Ureas. Simple Foldamers Equilibrate with Multiply Hydrogen-Bonded Sheetlike Structures1
    • Corbin, P. S.; Zimmerman, S. C.; Thiessen, P. A.; Hawryluk, N. A.; Murray, T. J. Complexation-Induced Unfolding of Heterocyclic Ureas. Simple Foldamers Equilibrate with Multiply Hydrogen-Bonded Sheetlike Structures1 J. Am. Chem. Soc. 2001, 123, 10475-10488 10.1021/ja010638q
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 10475-10488
    • Corbin, P.S.1    Zimmerman, S.C.2    Thiessen, P.A.3    Hawryluk, N.A.4    Murray, T.J.5
  • 151
    • 33947085959 scopus 로고
    • Conformations of Substituted Arylureas in Solution
    • Lepore, G.; Migdal, S.; Blagdon, D. E.; Goodman, M. Conformations of Substituted Arylureas in Solution J. Org. Chem. 1973, 38, 2590-2594 10.1021/jo00955a003
    • (1973) J. Org. Chem. , vol.38 , pp. 2590-2594
    • Lepore, G.1    Migdal, S.2    Blagdon, D.E.3    Goodman, M.4
  • 152
    • 15744365835 scopus 로고
    • Conformation of substituted arylureas. Crystal Structures of N,N'-dimethyl-N,N'-di(p-nitrophenyl)urea and N,N'-dimethyl-N,N'-di(2,4-dinitrophenyl)urea
    • Lepore, U.; Castronuovo Lepore, G.; Ganis, P.; Germain, G.; Goodman, M. Conformation of substituted arylureas. Crystal Structures of N,N'-dimethyl-N,N'-di(p-nitrophenyl)urea and N,N'-dimethyl-N,N'-di(2,4-dinitrophenyl)urea J. Org. Chem. 1976, 41, 2134-2137 10.1021/jo00874a014
    • (1976) J. Org. Chem. , vol.41 , pp. 2134-2137
    • Lepore, U.1    Castronuovo Lepore, G.2    Ganis, P.3    Germain, G.4    Goodman, M.5
  • 155
    • 2542569636 scopus 로고    scopus 로고
    • Polyaryl Anion Radicals via Alkali Metal Reduction of Arylurea Oligomers
    • Lewis, F. D.; Kurth, T. L.; Hattan, C. M.; Reiter, R. C.; Stevenson, C. D. Polyaryl Anion Radicals via Alkali Metal Reduction of Arylurea Oligomers Org. Lett. 2004, 6, 1605-1608 10.1021/ol0496069
    • (2004) Org. Lett. , vol.6 , pp. 1605-1608
    • Lewis, F.D.1    Kurth, T.L.2    Hattan, C.M.3    Reiter, R.C.4    Stevenson, C.D.5
  • 156
    • 34047217353 scopus 로고    scopus 로고
    • Synthesis and Stacked Conformations of Symmetrical and Unsymmetrical Oligo-ureas of Metaphenylenediamine
    • Clayden, J.; Lemiègre, L.; Helliwell, M. Synthesis and Stacked Conformations of Symmetrical and Unsymmetrical Oligo-ureas of Metaphenylenediamine J. Org. Chem. 2007, 72, 2302-2308 10.1021/jo061989w
    • (2007) J. Org. Chem. , vol.72 , pp. 2302-2308
    • Clayden, J.1    Lemiègre, L.2    Helliwell, M.3
  • 157
    • 57349142448 scopus 로고    scopus 로고
    • Helix Persistence and Breakdown in Oligoureas of Metaphenylenediamine: Apparent Diastereotopicity as a Spectroscopic Marker of Helix Length in Solution
    • Clayden, J.; Lemiègre, L.; Morris, G. A.; Pickworth, M.; Snape, T. J.; Jones, L. H. Helix Persistence and Breakdown in Oligoureas of Metaphenylenediamine: Apparent Diastereotopicity as a Spectroscopic Marker of Helix Length in Solution J. Am. Chem. Soc. 2008, 130, 15193-15202 10.1021/ja805758v
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 15193-15202
    • Clayden, J.1    Lemiègre, L.2    Morris, G.A.3    Pickworth, M.4    Snape, T.J.5    Jones, L.H.6
  • 158
    • 84936970816 scopus 로고    scopus 로고
    • Conformational Cooperativity between Helical Domains of Differing Geometry in Oligoamide-Oligourea Foldamer Chimeras
    • Maury, J.; Le Bailly, B. A. F.; Raftery, J.; Clayden, J. Conformational Cooperativity Between Helical Domains of Differing Geometry in Oligoamide-Oligourea Foldamer Chimeras Chem. Commun. 2015, 51, 11802-11805 10.1039/C5CC02995C
    • (2015) Chem. Commun. , vol.51 , pp. 11802-11805
    • Maury, J.1    Le Bailly, B.A.F.2    Raftery, J.3    Clayden, J.4
  • 160
    • 21344461945 scopus 로고    scopus 로고
    • P53 alpha-Helix Mimetics Antagonize p53/MDM2 Interaction and Activate p53
    • Chen, L.; Yin, H.; Farooqi, B.; Sebti, S.; Hamilton, A. D.; Chen, J. p53 alpha-Helix Mimetics Antagonize p53/MDM2 Interaction and Activate p53 Mol. Cancer Ther. 2005, 4, 1019-1025 10.1158/1535-7163.MCT-04-0342
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 1019-1025
    • Chen, L.1    Yin, H.2    Farooqi, B.3    Sebti, S.4    Hamilton, A.D.5    Chen, J.6
  • 163
    • 84924964570 scopus 로고    scopus 로고
    • Stereocontrolled Protein Surface Recognition Using Chiral Oligoamide Proteomimetic Foldamers
    • Azzarito, V.; Miles, J. A.; Fisher, J.; Edwards, T. A.; Warriner, S. L.; Wilson, A. J. Stereocontrolled Protein Surface Recognition Using Chiral Oligoamide Proteomimetic Foldamers Chem. Sci. 2015, 6, 2434-2443 10.1039/C4SC03559C
    • (2015) Chem. Sci. , vol.6 , pp. 2434-2443
    • Azzarito, V.1    Miles, J.A.2    Fisher, J.3    Edwards, T.A.4    Warriner, S.L.5    Wilson, A.J.6
  • 166
    • 0037048711 scopus 로고    scopus 로고
    • Development of a Potent Bcl-x(L) Antagonist Based on Alpha-Helix Mimicry
    • Kutzki, O.; Park, H. S.; Ernst, J. T.; Orner, B. P.; Yin, H.; Hamilton, A. D. Development of a Potent Bcl-x(L) Antagonist Based on Alpha-Helix Mimicry J. Am. Chem. Soc. 2002, 124, 11838-11839 10.1021/ja026861k
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11838-11839
    • Kutzki, O.1    Park, H.S.2    Ernst, J.T.3    Orner, B.P.4    Yin, H.5    Hamilton, A.D.6
  • 167
    • 33745181229 scopus 로고    scopus 로고
    • Development of Small Molecules Designed to Modulate Protein-Protein Interactions
    • Che, Y.; Brooks, B. R.; Marshall, G. R. Development of Small Molecules Designed to Modulate Protein-Protein Interactions J. Comput.-Aided Mol. Des. 2006, 20, 109-130 10.1007/s10822-006-9040-8
    • (2006) J. Comput.-Aided Mol. Des. , vol.20 , pp. 109-130
    • Che, Y.1    Brooks, B.R.2    Marshall, G.R.3
  • 168
    • 17644365389 scopus 로고    scopus 로고
    • Terephthalamide Derivatives as Mimetics of Helical Peptides: Disruption of the Bcl-x(L)/Bak Interaction
    • Yin, H.; Lee, G.-I.; Sedey, K. A.; Rodriguez, J. M.; Wang, H.-G.; Sebti, S. M.; Hamilton, A. D. Terephthalamide Derivatives as Mimetics of Helical Peptides: Disruption of the Bcl-x(L)/Bak Interaction J. Am. Chem. Soc. 2005, 127, 5463-5468 10.1021/ja0446404
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 5463-5468
    • Yin, H.1    Lee, G.-I.2    Sedey, K.A.3    Rodriguez, J.M.4    Wang, H.-G.5    Sebti, S.M.6    Hamilton, A.D.7
  • 169
    • 84901484924 scopus 로고    scopus 로고
    • Small-Molecule Proteomimetic Inhibitors of the HIF-1α-p300 Protein-Protein Interaction
    • Burslem, G. M.; Kyle, H. F.; Breeze, A. L.; Edwards, T. A.; Nelson, A.; Warriner, S. L.; Wilson, A. J. Small-Molecule Proteomimetic Inhibitors of the HIF-1α-p300 Protein-Protein Interaction ChemBioChem 2014, 15, 1083-1087 10.1002/cbic.201400009
    • (2014) ChemBioChem , vol.15 , pp. 1083-1087
    • Burslem, G.M.1    Kyle, H.F.2    Breeze, A.L.3    Edwards, T.A.4    Nelson, A.5    Warriner, S.L.6    Wilson, A.J.7
  • 170
    • 34250762561 scopus 로고    scopus 로고
    • Helix Mimetics as Inhibitors of the Interaction of the Estrogen Receptor with Coactivator Peptides
    • Becerril, J.; Hamilton, A. D. Helix Mimetics as Inhibitors of the Interaction of the Estrogen Receptor with Coactivator Peptides Angew. Chem., Int. Ed. 2007, 46, 4471-4473 10.1002/anie.200700657
    • (2007) Angew. Chem., Int. Ed. , vol.46 , pp. 4471-4473
    • Becerril, J.1    Hamilton, A.D.2
  • 171
    • 84859902380 scopus 로고    scopus 로고
    • A-kinase Anchoring Proteins as Potential Drug Targets
    • Tröger, J.; Moutty, M. C.; Skroblin, P.; Klussmann, E. A-kinase Anchoring Proteins as Potential Drug Targets Br. J. Pharmacol. 2012, 166, 420-433 10.1111/j.1476-5381.2011.01796.x
    • (2012) Br. J. Pharmacol. , vol.166 , pp. 420-433
    • Tröger, J.1    Moutty, M.C.2    Skroblin, P.3    Klussmann, E.4
  • 172
    • 0033582496 scopus 로고    scopus 로고
    • Protein Kinase A Anchoring Proteins are Required for Vasopressin-Mediated Translocation of Aquaporin-2 into Cell Membranes of Renal Principal Cells
    • Klussmann, E.; Maric, K.; Wiesner, B.; Beyermann, M.; Rosenthal, W. Protein Kinase A Anchoring Proteins are Required for Vasopressin-Mediated Translocation of Aquaporin-2 into Cell Membranes of Renal Principal Cells J. Biol. Chem. 1999, 274, 4934-4938 10.1074/jbc.274.8.4934
    • (1999) J. Biol. Chem. , vol.274 , pp. 4934-4938
    • Klussmann, E.1    Maric, K.2    Wiesner, B.3    Beyermann, M.4    Rosenthal, W.5
  • 173
    • 56549130084 scopus 로고    scopus 로고
    • AKAP220 Colocalizes with AQP2 in the Inner Medullary Collecting Ducts
    • Okutsu, R.; Rai, T.; Kikuchi, A.; Ohno, M.; Uchida, K.; Sasaki, S.; Uchida, S. AKAP220 Colocalizes with AQP2 in the Inner Medullary Collecting Ducts Kidney Int. 2008, 74, 1429-1433 10.1038/ki.2008.402
    • (2008) Kidney Int. , vol.74 , pp. 1429-1433
    • Okutsu, R.1    Rai, T.2    Kikuchi, A.3    Ohno, M.4    Uchida, K.5    Sasaki, S.6    Uchida, S.7
  • 175
    • 84865610004 scopus 로고    scopus 로고
    • Autocrine Regulation of Insulin Secretion
    • Braun, M.; Ramracheya, R.; Rorsman, P. Autocrine Regulation of Insulin Secretion Diabetes, Obes. Metab. 2012, 14, 143-151 10.1111/j.1463-1326.2012.01642.x
    • (2012) Diabetes, Obes. Metab. , vol.14 , pp. 143-151
    • Braun, M.1    Ramracheya, R.2    Rorsman, P.3
  • 176
    • 74849110603 scopus 로고    scopus 로고
    • Synthetic Alpha-Helix Mimetics as Agonists and Antagonists of Islet Amyloid Polypeptide Aggregation
    • Saraogi, I.; Hebda, J. A.; Becerril, J.; Estroff, L. A.; Miranker, A. D.; Hamilton, A. D. Synthetic Alpha-Helix Mimetics as Agonists and Antagonists of Islet Amyloid Polypeptide Aggregation Angew. Chem., Int. Ed. 2010, 49, 736-739 10.1002/anie.200901694
    • (2010) Angew. Chem., Int. Ed. , vol.49 , pp. 736-739
    • Saraogi, I.1    Hebda, J.A.2    Becerril, J.3    Estroff, L.A.4    Miranker, A.D.5    Hamilton, A.D.6
  • 177
    • 84925538053 scopus 로고    scopus 로고
    • Islet Amyloid-Induced Cell Death and Bilayer Integrity Loss Share a Molecular Origin Targetable with Oligopyridylamide-Based α-Helical Mimetics
    • Kumar, S.; Schlamadinger, D. E.; Brown, M. A.; Dunn, J. M.; Mercado, B.; Hebda, J. A.; Saraogi, I.; Rhoades, E.; Hamilton, A. D.; Miranker, A. D. Islet Amyloid-Induced Cell Death and Bilayer Integrity Loss Share a Molecular Origin Targetable with Oligopyridylamide-Based α-Helical Mimetics Chem. Biol. 2015, 22, 369-378 10.1016/j.chembiol.2015.01.006
    • (2015) Chem. Biol. , vol.22 , pp. 369-378
    • Kumar, S.1    Schlamadinger, D.E.2    Brown, M.A.3    Dunn, J.M.4    Mercado, B.5    Hebda, J.A.6    Saraogi, I.7    Rhoades, E.8    Hamilton, A.D.9    Miranker, A.D.10
  • 180
    • 0037015078 scopus 로고    scopus 로고
    • Direct Evidence for a G-Quadruplex in a Promoter Region and its Targeting with a Small Molecule to Repress c-MYC Transcription
    • Siddiqui-Jain, A.; Grand, C. L.; Bearss, D. J.; Hurley, L. H. Direct Evidence for a G-Quadruplex in a Promoter Region and its Targeting with a Small Molecule to Repress c-MYC Transcription Proc. Natl. Acad. Sci. U. S. A. 2002, 99, 11593-11598 10.1073/pnas.182256799
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 11593-11598
    • Siddiqui-Jain, A.1    Grand, C.L.2    Bearss, D.J.3    Hurley, L.H.4
  • 182
    • 34250776984 scopus 로고    scopus 로고
    • Development and Biological Assessment of Fully Water-Soluble Helical Aromatic Amide Foldamers
    • Gillies, E. R.; Deiss, F.; Staedel, C.; Schmitter, J.-M.; Huc, I. Development and Biological Assessment of Fully Water-Soluble Helical Aromatic Amide Foldamers Angew. Chem., Int. Ed. 2007, 46, 4081-4084 10.1002/anie.200700301
    • (2007) Angew. Chem., Int. Ed. , vol.46 , pp. 4081-4084
    • Gillies, E.R.1    Deiss, F.2    Staedel, C.3    Schmitter, J.-M.4    Huc, I.5
  • 183
    • 77955624117 scopus 로고    scopus 로고
    • Cellular Internalization of Water-Soluble Helical Aromatic Amide Foldamers
    • Iriondo-Alberdi, J.; Laxmi-Reddy, K.; Bouguerne, B.; Staedel, C.; Huc, I. Cellular Internalization of Water-Soluble Helical Aromatic Amide Foldamers ChemBioChem 2010, 11, 1679-1685 10.1002/cbic.201000256
    • (2010) ChemBioChem , vol.11 , pp. 1679-1685
    • Iriondo-Alberdi, J.1    Laxmi-Reddy, K.2    Bouguerne, B.3    Staedel, C.4    Huc, I.5
  • 184
    • 0024262589 scopus 로고
    • Cellular Uptake of the Tat Protein from Human Immunodeficiency Virus
    • Frankel, A. D.; Pabo, C. O. Cellular Uptake of the Tat Protein from Human Immunodeficiency Virus Cell 1988, 55, 1189-1193 10.1016/0092-8674(88)90263-2
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 185
    • 57049185166 scopus 로고    scopus 로고
    • De Novo Designed Synthetic Mimics of Antimicrobial Peptides
    • Scott, R. W.; DeGrado, W. F.; Tew, G. N. De Novo Designed Synthetic Mimics of Antimicrobial Peptides Curr. Opin. Biotechnol. 2008, 19, 620-627 10.1016/j.copbio.2008.10.013
    • (2008) Curr. Opin. Biotechnol. , vol.19 , pp. 620-627
    • Scott, R.W.1    DeGrado, W.F.2    Tew, G.N.3
  • 188
    • 33646064432 scopus 로고    scopus 로고
    • Biomimetic Facially Amphiphilic Antibacterial Oligomers with Conformationally stiff Backbones
    • Tang, H.; Doerksen, R. J.; Jones, T. V.; Klein, M. L.; Tew, G. N. Biomimetic Facially Amphiphilic Antibacterial Oligomers with Conformationally stiff Backbones Chem. Biol. 2006, 13, 427-435 10.1016/j.chembiol.2006.02.007
    • (2006) Chem. Biol. , vol.13 , pp. 427-435
    • Tang, H.1    Doerksen, R.J.2    Jones, T.V.3    Klein, M.L.4    Tew, G.N.5
  • 190
    • 84884961808 scopus 로고    scopus 로고
    • Investigational Antimicrobial Agents of 2013
    • Pucci, M. J.; Bush, K. Investigational Antimicrobial Agents of 2013 Clin. Microbiol. Rev. 2013, 26, 792-821 10.1128/CMR.00033-13
    • (2013) Clin. Microbiol. Rev. , vol.26 , pp. 792-821
    • Pucci, M.J.1    Bush, K.2
  • 191
    • 84876105389 scopus 로고    scopus 로고
    • Synthetic Oligoureas of Metaphenylenediamine Mimic Host Defence Peptides in their Antimicrobial Behaviour
    • Dennison, S. R.; Phoenix, D. A.; Snape, T. J. Synthetic Oligoureas of Metaphenylenediamine Mimic Host Defence Peptides in their Antimicrobial Behaviour Bioorg. Med. Chem. Lett. 2013, 23, 2518-2521 10.1016/j.bmcl.2013.03.018
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , pp. 2518-2521
    • Dennison, S.R.1    Phoenix, D.A.2    Snape, T.J.3
  • 192
    • 17444429937 scopus 로고    scopus 로고
    • Synthesis of Urea Oligomers and their Antibacterial Activity
    • Tang, H.; Doerksen, R. J.; Tew, G. N. Synthesis of Urea Oligomers and their Antibacterial Activity Chem. Commun. (Cambridge, U. K.) 2005, 1537-1539 10.1039/b413679a
    • (2005) Chem. Commun. (Cambridge, U. K.) , pp. 1537-1539
    • Tang, H.1    Doerksen, R.J.2    Tew, G.N.3
  • 193
    • 84895058088 scopus 로고    scopus 로고
    • Tuning the Guest-Binding Ability of a Helically Folded Capsule by in Situ Modification of the Aromatic Oligoamide Backbone
    • Lautrette, G.; Aube, C.; Ferrand, Y.; Pipelier, M.; Blot, V.; Thobie, C.; Kauffmann, B.; Dubreuil, D.; Huc, I. Tuning the Guest-Binding Ability of a Helically Folded Capsule by In Situ Modification of the Aromatic Oligoamide Backbone Chem.-Eur. J. 2014, 20, 1547-1553 10.1002/chem.201303929
    • (2014) Chem. - Eur. J. , vol.20 , pp. 1547-1553
    • Lautrette, G.1    Aube, C.2    Ferrand, Y.3    Pipelier, M.4    Blot, V.5    Thobie, C.6    Kauffmann, B.7    Dubreuil, D.8    Huc, I.9
  • 194
    • 84925773017 scopus 로고    scopus 로고
    • Iterative Design of a Helically Folded Aromatic Oligoamide Sequence for the Selective Encapsulation of Fructose
    • Chandramouli, N.; Ferrand, Y.; Lautrette, G.; Kauffmann, B.; Mackereth, C. D.; Laguerre, M.; Dubreuil, D.; Huc, I. Iterative Design of a Helically Folded Aromatic Oligoamide Sequence for the Selective Encapsulation of Fructose Nat. Chem. 2015, 7, 334-341 10.1038/nchem.2195
    • (2015) Nat. Chem. , vol.7 , pp. 334-341
    • Chandramouli, N.1    Ferrand, Y.2    Lautrette, G.3    Kauffmann, B.4    MacKereth, C.D.5    Laguerre, M.6    Dubreuil, D.7    Huc, I.8
  • 196
    • 27144443340 scopus 로고    scopus 로고
    • A Rapid Library Screen for Tailoring β-Peptide Structure and Function
    • Kritzer, J. A.; Luedtke, N. W.; Harker, E. A.; Schepartz, A. A Rapid Library Screen for Tailoring β-Peptide Structure and Function J. Am. Chem. Soc. 2005, 127, 14584-14585 10.1021/ja055050o
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 14584-14585
    • Kritzer, J.A.1    Luedtke, N.W.2    Harker, E.A.3    Schepartz, A.4
  • 197
    • 84879015546 scopus 로고    scopus 로고
    • Microwave Assisted Solid Phase Synthesis of Highly Functionalized N-Alkylated Oligobenzamide α-Helix Mimetics
    • Long, K.; Edwards, T. A.; Wilson, A. J. Microwave Assisted Solid Phase Synthesis of Highly Functionalized N-Alkylated Oligobenzamide α-Helix Mimetics Bioorg. Med. Chem. 2013, 21, 4034-4040 10.1016/j.bmc.2012.09.053
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 4034-4040
    • Long, K.1    Edwards, T.A.2    Wilson, A.J.3
  • 198
    • 0028916599 scopus 로고
    • A Hot Spot of Binding Energy in a Hormone-Receptor Interface
    • Clackson, T.; Wells, J. A. A Hot Spot of Binding Energy in a Hormone-Receptor Interface Science 1995, 267, 383-386 10.1126/science.7529940
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 199
    • 33744460279 scopus 로고    scopus 로고
    • Proteomimetic Libraries: Design, Synthesis, and Evaluation of p53-MDM2 Interaction Inhibitors
    • Lu, F.; Chi, S.-W.; Kim, D.-H.; Han, K.-H.; Kuntz, I. D.; Guy, R. K. Proteomimetic Libraries: Design, Synthesis, and Evaluation of p53-MDM2 Interaction Inhibitors J. Comb. Chem. 2006, 8, 315-325 10.1021/cc050142v
    • (2006) J. Comb. Chem. , vol.8 , pp. 315-325
    • Lu, F.1    Chi, S.-W.2    Kim, D.-H.3    Han, K.-H.4    Kuntz, I.D.5    Guy, R.K.6
  • 200
    • 84907997286 scopus 로고    scopus 로고
    • Improved PEP-FOLD Approach for Peptide and Miniprotein Structure Prediction
    • Shen, Y.; Maupetit, J.; Derreumaux, P.; Tufféry, P. Improved PEP-FOLD Approach for Peptide and Miniprotein Structure Prediction J. Chem. Theory Comput. 2014, 10, 4745-4758 10.1021/ct500592m
    • (2014) J. Chem. Theory Comput. , vol.10 , pp. 4745-4758
    • Shen, Y.1    Maupetit, J.2    Derreumaux, P.3    Tufféry, P.4
  • 201
    • 0345306764 scopus 로고    scopus 로고
    • Design of a Novel Globular Protein Fold with Atomic-Level Accuracy
    • Kuhlman, B.; Dantas, G.; Ireton, G. C.; Varani, G.; Stoddard, B. L.; Baker, D. Design of a Novel Globular Protein Fold with Atomic-Level Accuracy Science 2003, 302, 1364-1368 10.1126/science.1089427
    • (2003) Science , vol.302 , pp. 1364-1368
    • Kuhlman, B.1    Dantas, G.2    Ireton, G.C.3    Varani, G.4    Stoddard, B.L.5    Baker, D.6
  • 202
    • 84940721845 scopus 로고    scopus 로고
    • Fine Tuning of β-Peptide Foldamers: A Single Atom Replacement Holds Back the Switch from an 8-Helix to a 12-Helix
    • Altmayer-Henzien, A.; Declerck, V.; Farjon, J.; Merlet, D.; Guillot, R.; Aitken, D. J. Fine Tuning of β-Peptide Foldamers: a Single Atom Replacement Holds Back the Switch from an 8-Helix to a 12-Helix Angew. Chem., Int. Ed. 2015, 54, 10807-10810 10.1002/anie.201504126
    • (2015) Angew. Chem., Int. Ed. , vol.54 , pp. 10807-10810
    • Altmayer-Henzien, A.1    Declerck, V.2    Farjon, J.3    Merlet, D.4    Guillot, R.5    Aitken, D.J.6
  • 204
    • 77952786853 scopus 로고    scopus 로고
    • Protein Thermostability Calculations Using Alchemical Free Energy Simulations
    • Seeliger, D.; de Groot, B. L. Protein Thermostability Calculations Using Alchemical Free Energy Simulations Biophys. J. 2010, 98, 2309-2316 10.1016/j.bpj.2010.01.051
    • (2010) Biophys. J. , vol.98 , pp. 2309-2316
    • Seeliger, D.1    De Groot, B.L.2
  • 205
    • 84908255869 scopus 로고    scopus 로고
    • Predicting Order and Disorder for β-Peptide Foldamers in Water
    • Németh, L. J.; Hegedüs, Z.; Martinek, T. A. Predicting Order and Disorder for β-Peptide Foldamers in Water J. Chem. Inf. Model. 2014, 54, 2776-2783 10.1021/ci5003476
    • (2014) J. Chem. Inf. Model. , vol.54 , pp. 2776-2783
    • Németh, L.J.1    Hegedüs, Z.2    Martinek, T.A.3
  • 206
    • 84893899060 scopus 로고    scopus 로고
    • Solvent Effects on the Conformational Preferences of Model Peptoids. MP2 study
    • Wałȩsa, R.; Broda, M. A. Solvent Effects on the Conformational Preferences of Model Peptoids. MP2 study J. Pept. Sci. 2014, 20, 203-211 10.1002/psc.2601
    • (2014) J. Pept. Sci. , vol.20 , pp. 203-211
    • Wałȩsa, R.1    Broda, M.A.2
  • 207
    • 84871545594 scopus 로고    scopus 로고
    • Automation of the CHARMM General Force Field (CGenFF) I: Bond Perception and Atom Typing
    • Vanommeslaeghe, K.; MacKerell, A. D. Automation of the CHARMM General Force Field (CGenFF) I: Bond Perception and Atom Typing J. Chem. Inf. Model. 2012, 52, 3144-3154 10.1021/ci300363c
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 3144-3154
    • Vanommeslaeghe, K.1    MacKerell, A.D.2
  • 209
    • 84858266350 scopus 로고    scopus 로고
    • Incorporation of Noncanonical Amino Acids into Rosetta and Use in Computational Protein-Peptide Interface Design
    • Renfrew, P. D.; Choi, E. J.; Bonneau, R.; Kuhlman, B. Incorporation of Noncanonical Amino Acids into Rosetta and Use in Computational Protein-Peptide Interface Design PLoS One 2012, 7, e32637 10.1371/journal.pone.0032637
    • (2012) PLoS One , vol.7 , pp. e32637
    • Renfrew, P.D.1    Choi, E.J.2    Bonneau, R.3    Kuhlman, B.4
  • 210
    • 84890495015 scopus 로고    scopus 로고
    • Forcefield-PTM: Ab Initio Charge and AMBER Forcefield Parameters for Frequently Occurring Post-Translational Modifications
    • Khoury, G. A.; Thompson, J. P.; Smadbeck, J.; Kieslich, C. A.; Floudas, C. A. Forcefield-PTM: Ab Initio Charge and AMBER Forcefield Parameters for Frequently Occurring Post-Translational Modifications J. Chem. Theory Comput. 2013, 9, 5653-5674 10.1021/ct400556v
    • (2013) J. Chem. Theory Comput. , vol.9 , pp. 5653-5674
    • Khoury, G.A.1    Thompson, J.P.2    Smadbeck, J.3    Kieslich, C.A.4    Floudas, C.A.5
  • 214
    • 84908462496 scopus 로고    scopus 로고
    • Dendrimers in Drug Delivery and Targeting: Drug-dendrimer Interactions and Toxicity Issues
    • Madaan, K.; Kumar, S.; Poonia, N.; Lather, V.; Pandita, D. Dendrimers in Drug Delivery and Targeting: Drug-dendrimer Interactions and Toxicity Issues J. Pharm. BioAllied Sci. 2014, 6, 139-150 10.4103/0975-7406.130965
    • (2014) J. Pharm. BioAllied Sci. , vol.6 , pp. 139-150
    • Madaan, K.1    Kumar, S.2    Poonia, N.3    Lather, V.4    Pandita, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.