메뉴 건너뛰기




Volumn 13, Issue 1, 2005, Pages 11-16

β-Peptides as inhibitors of protein-protein interactions

Author keywords

Foldamer; Helix; Protein recognition; Proteomics

Indexed keywords

PEPTIDE DERIVATIVE; PROTEIN INHIBITOR; WATER;

EID: 9644273958     PISSN: 09680896     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmc.2004.09.009     Document Type: Short Survey
Times cited : (159)

References (57)
  • 1
    • 0003010660 scopus 로고    scopus 로고
    • Interaction, assembly and processing-at the chemistry-biology interface-overview
    • A. Schepartz, and P.S. Kim Interaction, assembly and processing-at the chemistry-biology interface-overview Curr. Opin. Chem. Biol. 2 1998 9
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 9
    • Schepartz, A.1    Kim, P.S.2
  • 5
    • 0035382627 scopus 로고    scopus 로고
    • The outstanding biological stability of beta- and gamma-peptides toward proteolytic enzymes: An in vitro investigation with fifteen peptidases
    • J. Frackenpohl, P.I. Arvidsson, J.V. Schreiber, and D. Seebach The outstanding biological stability of beta- and gamma-peptides toward proteolytic enzymes: an in vitro investigation with fifteen peptidases Chembiochem 2 2001 445
    • (2001) Chembiochem , vol.2 , pp. 445
    • Frackenpohl, J.1    Arvidsson, P.I.2    Schreiber, J.V.3    Seebach, D.4
  • 6
    • 0029953285 scopus 로고    scopus 로고
    • Beta-peptides: Synthesis by Arndt-Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X-ray crystallography. Helical secondary structure of a beta-hexapeptide in solution and its stability towards pepsin
    • D. Seebach, M. Overhand, F.N.M. Kuhnle, B. Martinoni, L. Oberer, U. Hommel, and H. Widmer Beta-peptides: synthesis by Arndt-Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X-ray crystallography. Helical secondary structure of a beta-hexapeptide in solution and its stability towards pepsin Helv. Chim. Acta 79 1996 913
    • (1996) Helv. Chim. Acta , vol.79 , pp. 913
    • Seebach, D.1    Overhand, M.2    Kuhnle, F.N.M.3    Martinoni, B.4    Oberer, L.5    Hommel, U.6    Widmer, H.7
  • 11
    • 0344443346 scopus 로고    scopus 로고
    • Molecular recognition of protein surfaces: High affinity ligands for the CBPKIX domain
    • S.E. Rutledge, H.M. Volkman, and A. Schepartz Molecular recognition of protein surfaces: high affinity ligands for the CBPKIX domain J. Am. Chem. Soc. 125 2003 14336
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14336
    • Rutledge, S.E.1    Volkman, H.M.2    Schepartz, A.3
  • 12
    • 0037467384 scopus 로고    scopus 로고
    • Miniature homeodomains: High specificity without an N-terminal arm
    • J.K. Montclare, and A. Schepartz Miniature homeodomains: high specificity without an N-terminal arm J. Am. Chem. Soc. 125 2003 3416
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3416
    • Montclare, J.K.1    Schepartz, A.2
  • 13
    • 0035886913 scopus 로고    scopus 로고
    • Design and evolution of a miniature bcl-2 binding protein
    • J.W. Chin, and A. Schepartz Design and evolution of a miniature bcl-2 binding protein Angew. Chem., Int. Ed. 40 2001 3806
    • (2001) Angew. Chem., Int. Ed. , vol.40 , pp. 3806
    • Chin, J.W.1    Schepartz, A.2
  • 14
    • 0035907464 scopus 로고    scopus 로고
    • Methodology for optimizing functional miniature proteins based on Avian pancreatic polypeptide using phage display
    • J.W. Chin, R.M. Grotzfeld, M.A. Fabian, and A. Schepartz Methodology for optimizing functional miniature proteins based on Avian pancreatic polypeptide using phage display Bioorg. Med. Chem. Lett. 11 2001 1501
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 1501
    • Chin, J.W.1    Grotzfeld, R.M.2    Fabian, M.A.3    Schepartz, A.4
  • 15
    • 0034811833 scopus 로고    scopus 로고
    • Concerted evolution of structure and function in a miniature protein
    • J.W. Chin, and A. Schepartz Concerted evolution of structure and function in a miniature protein J. Am. Chem. Soc. 123 2001 2929
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2929
    • Chin, J.W.1    Schepartz, A.2
  • 16
    • 0033612729 scopus 로고    scopus 로고
    • Highly specific DNA recognition by a designed miniature protein
    • N.J. Zondlo, and A. Schepartz Highly specific DNA recognition by a designed miniature protein J. Am. Chem. Soc. 121 1999 6938
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 6938
    • Zondlo, N.J.1    Schepartz, A.2
  • 18
  • 19
    • 0035471135 scopus 로고    scopus 로고
    • Beta-peptides: From structure to function
    • R.P. Cheng, S.H. Gellman, and W.F. DeGrado Beta-peptides: from structure to function Chem. Rev. 101 2001 3219
    • (2001) Chem. Rev. , vol.101 , pp. 3219
    • Cheng, R.P.1    Gellman, S.H.2    Degrado, W.F.3
  • 20
    • 0001452530 scopus 로고    scopus 로고
    • Beta(2)- and beta(3)-peptides with proteinaceous side chains: Synthesis and solution structures of constitutional isomers, a novel helical secondary structure and the influence of solvation and hydrophobic interactions on folding
    • D. Seebach, S. Abele, K. Gademann, G. Guichard, T. Hintermann, B. Jaun, J.L. Matthews, and J.V. Schreiber Beta(2)- and beta(3)-peptides with proteinaceous side chains: synthesis and solution structures of constitutional isomers, a novel helical secondary structure and the influence of solvation and hydrophobic interactions on folding Helv. Chim. Acta 81 1998 932
    • (1998) Helv. Chim. Acta , vol.81 , pp. 932
    • Seebach, D.1    Abele, S.2    Gademann, K.3    Guichard, G.4    Hintermann, T.5    Jaun, B.6    Matthews, J.L.7    Schreiber, J.V.8
  • 22
    • 0033960408 scopus 로고    scopus 로고
    • Structure and conformation of beta-oligopeptide derivatives with simple proteinogenic side chains: Circular dichroism and molecular dynamics investigations
    • D. Seebach, J.V. Schreiber, S. Abele, X. Daura, and W.F. van Gunsteren Structure and conformation of beta-oligopeptide derivatives with simple proteinogenic side chains: circular dichroism and molecular dynamics investigations Helv. Chim. Acta 83 2000 34
    • (2000) Helv. Chim. Acta , vol.83 , pp. 34
    • Seebach, D.1    Schreiber, J.V.2    Abele, S.3    Daura, X.4    Van Gunsteren, W.F.5
  • 23
    • 0000333938 scopus 로고    scopus 로고
    • Preparation of N-Fmoc-protected beta(2)- and beta(3)-amino acids and their use as building blocks for the solid-phase synthesis of beta-peptides
    • G. Guichard, S. Abele, and D. Seebach Preparation of N-Fmoc-protected beta(2)- and beta(3)-amino acids and their use as building blocks for the solid-phase synthesis of beta-peptides Helv. Chim. Acta 81 1998 187
    • (1998) Helv. Chim. Acta , vol.81 , pp. 187
    • Guichard, G.1    Abele, S.2    Seebach, D.3
  • 25
    • 0034803386 scopus 로고    scopus 로고
    • De novo design of a monomeric helical beta-peptide stabilized by electrostatic interactions
    • R.P. Cheng, and W.F. DeGrado De novo design of a monomeric helical beta-peptide stabilized by electrostatic interactions J. Am. Chem. Soc. 123 2001 5162
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5162
    • Cheng, R.P.1    Degrado, W.F.2
  • 26
    • 0035820415 scopus 로고    scopus 로고
    • Design, machine synthesis, and NMR-solution structure of a beta-heptapeptide forming a salt-bridge stabilised 3(14)-helix in methanol and in water
    • P.I. Arvidsson, M. Rueping, and D. Seebach Design, machine synthesis, and NMR-solution structure of a beta-heptapeptide forming a salt-bridge stabilised 3(14)-helix in methanol and in water Chem. Commun. 2001 649
    • (2001) Chem. Commun. , pp. 649
    • Arvidsson, P.I.1    Rueping, M.2    Seebach, D.3
  • 27
    • 0037032269 scopus 로고    scopus 로고
    • Can one derive the conformational preference of a beta-peptide from its CD spectrum?
    • A. Glattli, X. Daura, D. Seebach, and W.F. van Gunsteren Can one derive the conformational preference of a beta-peptide from its CD spectrum? J. Am. Chem. Soc. 124 2002 12972
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 12972
    • Glattli, A.1    Daura, X.2    Seebach, D.3    Van Gunsteren, W.F.4
  • 28
    • 0038411295 scopus 로고    scopus 로고
    • Syntheses and CD-spectroscopic investigations of longer-chain beta-peptides: Preparation by solid-phase couplings of single amino acids, dipeptides, and tripeptides
    • P.I. Arvidsson, J. Frackenpohl, and D. Seebach Syntheses and CD-spectroscopic investigations of longer-chain beta-peptides: preparation by solid-phase couplings of single amino acids, dipeptides, and tripeptides Helv. Chim. Acta 86 2003 1522
    • (2003) Helv. Chim. Acta , vol.86 , pp. 1522
    • Arvidsson, P.I.1    Frackenpohl, J.2    Seebach, D.3
  • 29
    • 0038713800 scopus 로고    scopus 로고
    • Accommodation of alpha-substituted residues in the beta-peptide 12-helix: Expanding the range of substitution patterns available to a foldamer scaffold
    • J.S. Park, H.S. Lee, J.R. Lai, B.M. Kim, and S.H. Gellman Accommodation of alpha-substituted residues in the beta-peptide 12-helix: expanding the range of substitution patterns available to a foldamer scaffold J. Am. Chem. Soc. 125 2003 8539
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8539
    • Park, J.S.1    Lee, H.S.2    Lai, J.R.3    Kim, B.M.4    Gellman, S.H.5
  • 30
    • 0037959630 scopus 로고    scopus 로고
    • Environment-independent 14-helix formation in short beta-peptides: Striking a balance between shape control and functional diversity
    • T.L. Raguse, J.R. Lai, and S.H. Gellman Environment-independent 14-helix formation in short beta-peptides: Striking a balance between shape control and functional diversity J. Am. Chem. Soc. 125 2003 5592
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5592
    • Raguse, T.L.1    Lai, J.R.2    Gellman, S.H.3
  • 31
    • 0037010015 scopus 로고    scopus 로고
    • Long-range interactions stabilize the fold of a non-natural oligomer
    • R.P. Cheng, and W.F. DeGrado Long-range interactions stabilize the fold of a non-natural oligomer J. Am. Chem. Soc. 124 2002 11564
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11564
    • Cheng, R.P.1    Degrado, W.F.2
  • 32
    • 0027524623 scopus 로고
    • Charged histidine affects alpha-helix stability at all positions in the helix by interacting with the backbone charges
    • K.M. Armstrong, and R.L. Baldwin Charged histidine affects alpha-helix stability at all positions in the helix by interacting with the backbone charges Proc. Natl. Acad. Sci. U.S.A. 90 1993 11337
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 11337
    • Armstrong, K.M.1    Baldwin, R.L.2
  • 33
    • 0024506404 scopus 로고
    • Further studies of the helix dipole model: Effects of a free alpha-Nh3+ or alpha-COO- group on helix stability
    • R. Fairman, K.R. Shoemaker, E.J. York, J.M. Stewart, and R.L. Baldwin Further studies of the helix dipole model: effects of a free alpha-Nh3+ or alpha-COO- group on helix stability Proteins 5 1989 1
    • (1989) Proteins , vol.5 , pp. 1
    • Fairman, R.1    Shoemaker, K.R.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 34
    • 0027912723 scopus 로고
    • Electrostatic screening of charge and dipole interactions with the helix backbone
    • D.J. Lockhart, and P.S. Kim Electrostatic screening of charge and dipole interactions with the helix backbone Science 260 1993 198
    • (1993) Science , vol.260 , pp. 198
    • Lockhart, D.J.1    Kim, P.S.2
  • 35
  • 39
    • 0037609791 scopus 로고    scopus 로고
    • Protein-protein interactions: Structurally conserved residues distinguish between binding sites and exposed protein surfaces
    • B.Y. Ma, T. Elkayam, H. Wolfson, and R. Nussinov Protein-protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces Proc. Natl. Acad. Sci. U.S.A. 100 2003 5772
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 5772
    • Ma, B.Y.1    Elkayam, T.2    Wolfson, H.3    Nussinov, R.4
  • 40
    • 0033519190 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of a cyclo-beta-tetrapeptide as a somatostatin analogue
    • K. Gademann, M. Ernst, D. Hoyer, and D. Seebach Synthesis and biological evaluation of a cyclo-beta-tetrapeptide as a somatostatin analogue Angew. Chem., Int. Ed. 38 1999 1223
    • (1999) Angew. Chem., Int. Ed. , vol.38 , pp. 1223
    • Gademann, K.1    Ernst, M.2    Hoyer, D.3    Seebach, D.4
  • 41
    • 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
    • K. Gademann, T. Kimmerlin, D. Hoyer, and D. Seebach Peptide folding induces high and selective affinity of a linear and small beta-peptide to the human somatostatin receptor 4 J. Med. Chem. 44 2001 2460
    • (2001) J. Med. Chem. , vol.44 , pp. 2460
    • Gademann, K.1    Kimmerlin, T.2    Hoyer, D.3    Seebach, D.4
  • 42
    • 0032881267 scopus 로고    scopus 로고
    • Beta-peptides as inhibitors of small-intestinal cholesterol and fat absorption
    • M. Werder, H. Hauser, S. Abele, and D. Seebach Beta-peptides as inhibitors of small-intestinal cholesterol and fat absorption Helv. Chim. Acta 82 1999 1774
    • (1999) Helv. Chim. Acta , vol.82 , pp. 1774
    • Werder, M.1    Hauser, H.2    Abele, S.3    Seebach, D.4
  • 44
    • 0034802565 scopus 로고    scopus 로고
    • De novo design, synthesis, and characterization of antimicrobial beta-peptides
    • D.H. Liu, and W.F. DeGrado De novo design, synthesis, and characterization of antimicrobial beta-peptides J. Am. Chem. Soc. 123 2001 7553
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7553
    • Liu, D.H.1    Degrado, W.F.2
  • 46
    • 0347417960 scopus 로고    scopus 로고
    • Antibiotic and hemolytic activity of a beta(2)/beta(3) peptide capable of folding into a 12/10-helical secondary structure
    • P.I. Arvidsson, N.S. Ryder, H.M. Weiss, G. Gross, O. Kretz, R. Woessner, and D. Seebach Antibiotic and hemolytic activity of a beta(2)/beta(3) peptide capable of folding into a 12/10-helical secondary structure Chembiochem 4 2003 1345
    • (2003) Chembiochem , vol.4 , pp. 1345
    • Arvidsson, P.I.1    Ryder, N.S.2    Weiss, H.M.3    Gross, G.4    Kretz, O.5    Woessner, R.6    Seebach, D.7
  • 49
    • 0033959744 scopus 로고    scopus 로고
    • MDM2-master regulator of the p53 tumor suppressor protein
    • J. Momand, H.H. Wu, and G. Dasgupta MDM2-master regulator of the p53 tumor suppressor protein Gene 242 2000 15
    • (2000) Gene , vol.242 , pp. 15
    • Momand, J.1    Wu, H.H.2    Dasgupta, G.3
  • 52
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • P. Guntert, C. Mumenthaler, and K. Wuthrich Torsion angle dynamics for NMR structure calculation with the new program DYANA J. Mol. Biol. 273 1997 283
    • (1997) J. Mol. Biol. , vol.273 , pp. 283
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 53
    • 0029896175 scopus 로고    scopus 로고
    • One bead-one compound combinatorial peptide library: Different types of screening
    • C.L. Chen, P. Strop, M. Lebl, and K.S. Lam One bead-one compound combinatorial peptide library: different types of screening Methods Enzymol. 267 1996 211
    • (1996) Methods Enzymol. , vol.267 , pp. 211
    • Chen, C.L.1    Strop, P.2    Lebl, M.3    Lam, K.S.4
  • 55
    • 0000577984 scopus 로고    scopus 로고
    • The 'one-bead-one-compound' combinatorial library method
    • K.S. Lam, M. Lebl, and V. Krchnak The 'one-bead-one-compound' combinatorial library method Chem. Rev. 97 1997 411
    • (1997) Chem. Rev. , vol.97 , pp. 411
    • Lam, K.S.1    Lebl, M.2    Krchnak, V.3
  • 56
    • 0242415199 scopus 로고    scopus 로고
    • Efficient and sequence-specific DNA-templated polymerization of peptide nucleic acid aldehydes
    • D.M. Rosenbaum, and D.R. Liu Efficient and sequence-specific DNA-templated polymerization of peptide nucleic acid aldehydes J. Am. Chem. Soc. 125 2004 13924
    • (2004) J. Am. Chem. Soc. , vol.125 , pp. 13924
    • Rosenbaum, D.M.1    Liu, D.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.