메뉴 건너뛰기




Volumn 117, Issue 47, 2013, Pages 12350-12362

Cyclic constraints on conformational flexibility in γ-peptides: Conformation specific IR and UV spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RESIDUES; CONFORMATIONAL FLEXIBILITY; CONFORMATIONAL PREFERENCES; HYDROGEN-BONDED STRUCTURES; NEAREST-NEIGHBORS; PEPTIDE BACKBONES; SUBSTITUTION PATTERNS; TWO PHOTON IONIZATION;

EID: 84886634658     PISSN: 10895639     EISSN: 15205215     Source Type: Journal    
DOI: 10.1021/jp408736t     Document Type: Article
Times cited : (28)

References (53)
  • 2
    • 0542421525 scopus 로고    scopus 로고
    • Foldamers: A Manifesto
    • Gellman, S. H. Foldamers: A Manifesto Acc. Chem. Res. 1998, 31 (4) 173-180
    • (1998) Acc. Chem. Res. , vol.31 , Issue.4 , pp. 173-180
    • Gellman, S.H.1
  • 3
    • 34247362490 scopus 로고    scopus 로고
    • Foldamers as Versatile Frameworks for the Design and Evolution of Function
    • Goodman, C. M.; Choi, S.; Shandler, S.; DeGrado, W. F. Foldamers as Versatile Frameworks for the Design and Evolution of Function Nat Chem Biol 2007, 3 (5) 252-262
    • (2007) Nat Chem Biol , vol.3 , Issue.5 , pp. 252-262
    • Goodman, C.M.1    Choi, S.2    Shandler, S.3    Degrado, W.F.4
  • 4
    • 79956128878 scopus 로고    scopus 로고
    • Synthetic Foldamers
    • Guichard, G.; Huc, I. Synthetic Foldamers Chem. Commun. 2011, 47 (21) 5933-5941
    • (2011) Chem. Commun. , vol.47 , Issue.21 , pp. 5933-5941
    • Guichard, G.1    Huc, I.2
  • 5
  • 6
    • 0029953285 scopus 로고    scopus 로고
    • β-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 β-Hexapeptide in Solution and its Stability owards Pepsin
    • Seebach, D.; Overhand, M.; Kühnle, F. N. M.; Martinoni, B.; Oberer, L.; Hommel, U.; Widmer, H. β-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 β-Hexapeptide in Solution and its Stability owards Pepsin Helv. Chim. Acta 1996, 79 (4) 913-941
    • (1996) Helv. Chim. Acta , vol.79 , Issue.4 , pp. 913-941
    • Seebach, D.1    Overhand, M.2    Kühnle, F.N.M.3    Martinoni, B.4    Oberer, L.5    Hommel, U.6    Widmer, H.7
  • 7
    • 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 (51) 13071-13072
    • (1996) J. Am. Chem. Soc. , vol.118 , Issue.51 , pp. 13071-13072
    • Appella, D.H.1    Christianson, L.A.2    Karle, I.L.3    Powell, D.R.4    Gellman, S.H.5
  • 8
    • 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 (33) 8569-8570
    • (1998) J. Am. Chem. Soc. , vol.120 , Issue.33 , pp. 8569-8570
    • Hanessian, S.1    Luo, X.2    Schaum, R.3    Michnick, S.4
  • 10
    • 84862889411 scopus 로고    scopus 로고
    • 4-Hybrid Peptide Helices: Synthesis, Crystal Conformations and Analogy with the α-Helix
    • 4-Hybrid Peptide Helices: Synthesis, Crystal Conformations and Analogy with the α-Helix Chem. Commun. 2012, 48 (57) 7170-7172
    • (2012) Chem. Commun. , vol.48 , Issue.57 , pp. 7170-7172
    • Bandyopadhyay, A.1    Jadhav, S.V.2    Gopi, H.N.3
  • 11
    • 84865419850 scopus 로고    scopus 로고
    • Structural Characterization of Backbone-Expanded Helices in Hybrid Peptides: (αγ)n and (αβ)n Sequences with Unconstrained β and γ Homologues of L-Val
    • Basuroy, K.; Dinesh, B.; Shamala, N.; Balaram, P. Structural Characterization of Backbone-Expanded Helices in Hybrid Peptides: (αγ)n and (αβ)n Sequences with Unconstrained β and γ Homologues of L-Val Angew. Chem., Int. Ed. 2012, 51 (35) 8736-8739
    • (2012) Angew. Chem., Int. Ed. , vol.51 , Issue.35 , pp. 8736-8739
    • Basuroy, K.1    Dinesh, B.2    Shamala, N.3    Balaram, P.4
  • 12
    • 84861796554 scopus 로고    scopus 로고
    • Hybrid Peptides: Direct Transformation of α/α, β-Unsaturated γ-Hybrid Peptides to α/γ-Hybrid Peptide 12-Helices
    • Bandyopadhyay, A.; Gopi, H. N. Hybrid Peptides: Direct Transformation of α/α, β-Unsaturated γ-Hybrid Peptides to α/γ-Hybrid Peptide 12-Helices Org. Lett. 2012, 14 (11) 2770-2773
    • (2012) Org. Lett. , vol.14 , Issue.11 , pp. 2770-2773
    • Bandyopadhyay, A.1    Gopi, H.N.2
  • 13
    • 84871103155 scopus 로고    scopus 로고
    • 4-Hybrid Peptide12-Helices with Proteinogenic Side Chains and their Analogy with α- And β-Peptide Helices
    • 4-Hybrid Peptide12-Helices with Proteinogenic Side Chains and their Analogy with α- and β-Peptide Helices Org. Biomol. Chem. 2013, 11 (3) 509-514
    • (2013) Org. Biomol. Chem. , vol.11 , Issue.3 , pp. 509-514
    • Jadhav, S.V.1    Bandyopadhyay, A.2    Gopi, H.N.3
  • 15
  • 16
    • 0035924947 scopus 로고    scopus 로고
    • Preparation and Determination of X-Ray-Crystal and NMR-Solution Structures of γ-Peptides
    • Seebach, D.; Brenner, M.; Rueping, M.; Schweizer, B.; Jaun, B. Preparation and Determination of X-Ray-Crystal and NMR-Solution Structures of γ-Peptides Chem. Commun. 2001, 2, 207-208
    • (2001) Chem. Commun. , vol.2 , pp. 207-208
    • Seebach, D.1    Brenner, M.2    Rueping, M.3    Schweizer, B.4    Jaun, B.5
  • 17
    • 0037006239 scopus 로고    scopus 로고
    • 2,3,4- Amino Acids, Coupling to γ-Hexapeptides: CD Spectra, NMR Solution and X-ray Crystal Structures of γ-Peptides
    • 2,3,4-Amino Acids, Coupling to γ-Hexapeptides: CD Spectra, NMR Solution and X-ray Crystal Structures of γ-Peptides Chem. - Euro. J. 2002, 8 (3) 573-584
    • (2002) Chem. - Euro. J. , vol.8 , Issue.3 , pp. 573-584
    • Seebach, D.1    Brenner, M.2    Rueping, M.3    Jaun, B.4
  • 18
    • 84961974533 scopus 로고    scopus 로고
    • Helix Formation and Folding in γ-Peptides and Their Vinylogues
    • Baldauf, C.; Günther, R.; Hofmann, H.-J. Helix Formation and Folding in γ-Peptides and Their Vinylogues Helv. Chim. Acta 2003, 86 (7) 2573-2588
    • (2003) Helv. Chim. Acta , vol.86 , Issue.7 , pp. 2573-2588
    • Baldauf, C.1    Günther, R.2    Hofmann, H.-J.3
  • 19
    • 70350334964 scopus 로고    scopus 로고
    • Gabapentin: A Stereochemically Constrained γ Amino Acid Residue in Hybrid Peptide Design
    • Vasudev, P. G.; Chatterjee, S.; Shamala, N.; Balaram, P. Gabapentin: A Stereochemically Constrained γ Amino Acid Residue in Hybrid Peptide Design Acc. Chem. Res. 2009, 42 (10) 1628-1639
    • (2009) Acc. Chem. Res. , vol.42 , Issue.10 , pp. 1628-1639
    • Vasudev, P.G.1    Chatterjee, S.2    Shamala, N.3    Balaram, P.4
  • 20
    • 79951650747 scopus 로고    scopus 로고
    • Structural Chemistry of Peptides Containing Backbone Expanded Amino Acid Residues: Conformational Features of β, γ, and Hybrid Peptides
    • Vasudev, P. G.; Chatterjee, S.; Shamala, N.; Balaram, P. Structural Chemistry of Peptides Containing Backbone Expanded Amino Acid Residues: Conformational Features of β, γ, and Hybrid Peptides Chem. Rev. 2010, 111 (2) 657-687
    • (2010) Chem. Rev. , vol.111 , Issue.2 , pp. 657-687
    • Vasudev, P.G.1    Chatterjee, S.2    Shamala, N.3    Balaram, P.4
  • 23
    • 70149086257 scopus 로고    scopus 로고
    • Single-Conformation and Diastereomer Specific Ultraviolet and Infrared Spectroscopy of Model Synthetic Foldamers: α/β-Peptides
    • James, W. H., III; Baquero, E. E.; Shubert, V. A.; Choi, S. H.; Gellman, S. H.; Zwier, T. S. Single-Conformation and Diastereomer Specific Ultraviolet and Infrared Spectroscopy of Model Synthetic Foldamers: α/β-Peptides J. Am. Chem. Soc. 2009, 131 (18) 6574-6590
    • (2009) J. Am. Chem. Soc. , vol.131 , Issue.18 , pp. 6574-6590
    • James III, W.H.1    Baquero, E.E.2    Shubert, V.A.3    Choi, S.H.4    Gellman, S.H.5    Zwier, T.S.6
  • 24
    • 77249161758 scopus 로고    scopus 로고
    • Laser Spectroscopy of Conformationally Constrained α/β- Peptides: Ac-ACPC-Phe-NHMe and Ac-Phe-ACPC-NHMe†
    • James, W. H., III; Baquero, E. E.; Choi, S. H.; Gellman, S. H.; Zwier, T. S. Laser Spectroscopy of Conformationally Constrained α/β-Peptides: Ac-ACPC-Phe-NHMe and Ac-Phe-ACPC-NHMe† J. Chem. Phys. A 2009, 114 (3) 1581-1591
    • (2009) J. Chem. Phys. A , vol.114 , Issue.3 , pp. 1581-1591
    • James III, W.H.1    Baquero, E.E.2    Choi, S.H.3    Gellman, S.H.4    Zwier, T.S.5
  • 26
    • 80055034138 scopus 로고    scopus 로고
    • Competition between Amide Stacking and Intramolecular H Bonds in γ-Peptide Derivatives: Controlling Nearest-Neighbor Preferences
    • James, W. H., III; Buchanan, E. G.; Guo, L.; Gellman, S. H.; Zwier, T. S. Competition between Amide Stacking and Intramolecular H Bonds in γ-Peptide Derivatives: Controlling Nearest-Neighbor Preferences J. Chem. Phys. A 2011, 115 (43) 11960-11970
    • (2011) J. Chem. Phys. A , vol.115 , Issue.43 , pp. 11960-11970
    • James III, W.H.1    Buchanan, E.G.2    Guo, L.3    Gellman, S.H.4    Zwier, T.S.5
  • 28
    • 79960177761 scopus 로고    scopus 로고
    • Single-Conformation Spectroscopy and Population Analysis of Model γ-Peptides: New Tests of Amide Stacking
    • Buchanan, E. G.; James, W. H., III; Gutberlet, A.; Dean, J. C.; Guo, L.; Gellman, S. H.; Zwier, T. S. Single-Conformation Spectroscopy and Population Analysis of Model γ-Peptides: New Tests of Amide Stacking Faraday Discuss. 2011, 150 (0) 209-226
    • (2011) Faraday Discuss. , vol.150 , Issue.0 , pp. 209-226
    • Buchanan, E.G.1    James III, W.H.2    Gutberlet, A.3    Dean, J.C.4    Guo, L.5    Gellman, S.H.6    Zwier, T.S.7
  • 29
    • 70450162565 scopus 로고    scopus 로고
    • Stereospecific Synthesis of Conformationally Constrained γ-Amino Acids: New Foldamer Building Blocks That Support Helical Secondary Structure
    • Guo, L.; Chi, Y.; Almeida, A. M.; Guzei, I. A.; Parker, B. K.; Gellman, S. H. Stereospecific Synthesis of Conformationally Constrained γ-Amino Acids: New Foldamer Building Blocks That Support Helical Secondary Structure J. Am. Chem. Soc. 2009, 131 (44) 16018-16020
    • (2009) J. Am. Chem. Soc. , vol.131 , Issue.44 , pp. 16018-16020
    • Guo, L.1    Chi, Y.2    Almeida, A.M.3    Guzei, I.A.4    Parker, B.K.5    Gellman, S.H.6
  • 30
    • 84994995581 scopus 로고
    • Analytical Multiphoton Ionization Mass Spectrometry. Part II. Applications
    • Lubman, D. M. Analytical Multiphoton Ionization Mass Spectrometry. Part II. Applications Mass Spectrom. Rev. 1988, 7, 559-592
    • (1988) Mass Spectrom. Rev. , vol.7 , pp. 559-592
    • Lubman, D.M.1
  • 31
    • 36549092485 scopus 로고
    • Local Modes of Benzene and Benzene Dimer, Studied by Infrared - Ultraviolet Double Resonance in a Supersonic Beam
    • Page, R. H.; Shen, Y. R.; Lee, Y. T. Local Modes of Benzene and Benzene Dimer, Studied by Infrared - Ultraviolet Double Resonance in a Supersonic Beam J. Chem. Phys. 1988, 88 (8) 4621-4636
    • (1988) J. Chem. Phys. , vol.88 , Issue.8 , pp. 4621-4636
    • Page, R.H.1    Shen, Y.R.2    Lee, Y.T.3
  • 32
    • 0035807680 scopus 로고    scopus 로고
    • Laser Spectroscopy of Jet-Cooled Biomolecules and Their Water-Containing Clusters: Water Bridges and Molecular Conformation
    • Zwier, T. S. Laser Spectroscopy of Jet-Cooled Biomolecules and Their Water-Containing Clusters: Water Bridges and Molecular Conformation J. Chem. Phys. A 2001, 105 (39) 8827-8839
    • (2001) J. Chem. Phys. A , vol.105 , Issue.39 , pp. 8827-8839
    • Zwier, T.S.1
  • 33
    • 0000243031 scopus 로고    scopus 로고
    • The Spectroscopy of Solvation in Hydrogen-Bonded Aromatic Clusters
    • Zwier, T. S. The Spectroscopy of Solvation in Hydrogen-Bonded Aromatic Clusters Annu. Rev. Phys. Chem. 1996, 47 (1) 205-241
    • (1996) Annu. Rev. Phys. Chem. , vol.47 , Issue.1 , pp. 205-241
    • Zwier, T.S.1
  • 35
    • 84986518863 scopus 로고
    • Amber - Assisted Model-Building with Energy Refinement - A General Program for Modeling Molecules and Their Interactions
    • Weiner, P. K.; Kollman, P. A. Amber-Assisted Model-Building with Energy Refinement-a General Program for Modeling Molecules and Their Interactions J. Comput. Chem. 1981, 2 (3) 287-303
    • (1981) J. Comput. Chem. , vol.2 , Issue.3 , pp. 287-303
    • Weiner, P.K.1    Kollman, P.A.2
  • 36
    • 34249288385 scopus 로고    scopus 로고
    • Density Functionals for Noncovalent Interaction Energies of Biological Importance
    • Zhao, Y.; Truhlar, D. G. Density Functionals for Noncovalent Interaction Energies of Biological Importance J. Chem. Theory Comput. 2007, 3 (1) 289-300
    • (2007) J. Chem. Theory Comput. , vol.3 , Issue.1 , pp. 289-300
    • Zhao, Y.1    Truhlar, D.G.2
  • 38
    • 84866103527 scopus 로고    scopus 로고
    • Single-Conformation Infrared Spectra of Model Peptides in the Amide i and Amide II Regions: Experiment-Based Determination of Local Mode Frequencies and Inter-Mode Coupling
    • Buchanan, E. G.; James, W. H., III; Choi, S. H.; Guo, L.; Gellman, S. H.; Muller, C. W.; Zwier, T. S. Single-Conformation Infrared Spectra of Model Peptides in the Amide I and Amide II Regions: Experiment-Based Determination of Local Mode Frequencies and Inter-Mode Coupling J. Chem. Phys. 2012, 137 (9) 094301-094316
    • (2012) J. Chem. Phys. , vol.137 , Issue.9 , pp. 094301-094316
    • Buchanan, E.G.1    James III, W.H.2    Choi, S.H.3    Guo, L.4    Gellman, S.H.5    Muller, C.W.6    Zwier, T.S.7
  • 43
    • 79952762339 scopus 로고    scopus 로고
    • Isolated Monohydrates of a Model Peptide Chain: Effect of a First Water Molecule on the Secondary Structure of a Capped Phenylalanine
    • Biswal, H. S.; Loquais, Y.; Tardivel, B.; Gloaguen, E.; Mons, M. Isolated Monohydrates of a Model Peptide Chain: Effect of a First Water Molecule on the Secondary Structure of a Capped Phenylalanine J. Am. Chem. Soc. 2011, 133 (11) 3931-3942
    • (2011) J. Am. Chem. Soc. , vol.133 , Issue.11 , pp. 3931-3942
    • Biswal, H.S.1    Loquais, Y.2    Tardivel, B.3    Gloaguen, E.4    Mons, M.5
  • 44
    • 0003341629 scopus 로고
    • Molecular Vibrational Frequencies
    • Linstrom, P. J. Mallard, W. G. National Institute of Standards and Technology: Gaithersburg, MD
    • Shimanouchi, T., Molecular Vibrational Frequencies. In NIST Chemistry WebBook, NIST Standard Reference Database Number 69; Linstrom, P. J.; Mallard, W. G., Eds.; National Institute of Standards and Technology: Gaithersburg, MD, 1972.
    • (1972) NIST Chemistry WebBook, NIST Standard Reference Database Number 69
    • Shimanouchi, T.1
  • 46
    • 33644583896 scopus 로고    scopus 로고
    • Helices and Other Secondary Structures of β- And γ-Peptides
    • Seebach, D.; Hook, D. F.; Glättli, A. Helices and Other Secondary Structures of β- and γ-Peptides Peptide Sci. 2006, 84 (1) 23-37
    • (2006) Peptide Sci. , vol.84 , Issue.1 , pp. 23-37
    • Seebach, D.1    Hook, D.F.2    Glättli, A.3
  • 47
    • 84869468145 scopus 로고    scopus 로고
    • Far/Mid-Infrared Signatures of Solvent-Solute Interactions in a Microhydrated Model Peptide Chain
    • Cirtog, M.; Rijs, A. M.; Loquais, Y.; Brenner, V.; Tardivel, B.; Gloaguen, E.; Mons, M. Far/Mid-Infrared Signatures of Solvent-Solute Interactions in a Microhydrated Model Peptide Chain J. Chem. Phys. Lett. 2012, 3 (22) 3307-3311
    • (2012) J. Chem. Phys. Lett. , vol.3 , Issue.22 , pp. 3307-3311
    • Cirtog, M.1    Rijs, A.M.2    Loquais, Y.3    Brenner, V.4    Tardivel, B.5    Gloaguen, E.6    Mons, M.7
  • 48
    • 67650333083 scopus 로고    scopus 로고
    • Jet-Cooled Electronic and Vibrational Spectroscopy of Crown Ethers: Benzo-15-Crown-5 Ether and 4′-Amino-Benzo-15-Crown-5 Ether
    • Shubert, V. A.; James, W. H.; Zwier, T. S. Jet-Cooled Electronic and Vibrational Spectroscopy of Crown Ethers: Benzo-15-Crown-5 Ether and 4′-Amino-Benzo-15-Crown-5 Ether J. Chem. Phys. A 2009, 113 (28) 8055-8066
    • (2009) J. Chem. Phys. A , vol.113 , Issue.28 , pp. 8055-8066
    • Shubert, V.A.1    James, W.H.2    Zwier, T.S.3
  • 50
    • 84914202563 scopus 로고    scopus 로고
    • Purdue University, West Lafayette, IN
    • James, W. H., III. Dissertation. Purdue University, West Lafayette, IN, 2009.
    • (2009) Dissertation
    • James III, W.H.1
  • 51
    • 84878656047 scopus 로고    scopus 로고
    • Differential Impact of β and γ Residue Preorganization on α/β/γ-Peptide Helix Stability in Water
    • Shin, Y.-H.; Mortenson, D. E.; Satyshur, K. A.; Forest, K. T.; Gellman, S. H. Differential Impact of β and γ Residue Preorganization on α/β/γ-Peptide Helix Stability in Water J. Am. Chem. Soc. 2013, 135 (22) 8149-8152
    • (2013) J. Am. Chem. Soc. , vol.135 , Issue.22 , pp. 8149-8152
    • Shin, Y.-H.1    Mortenson, D.E.2    Satyshur, K.A.3    Forest, K.T.4    Gellman, S.H.5
  • 52
    • 79955921951 scopus 로고    scopus 로고
    • Structural Mimicry of the α-Helix in Aqueous Solution with an Isoatomic α/β/γ-Peptide Backbone
    • Sawada, T.; Gellman, S. H. Structural Mimicry of the α-Helix in Aqueous Solution with an Isoatomic α/β/γ-Peptide Backbone J. Am. Chem. Soc. 2011, 133 (19) 7336-7339
    • (2011) J. Am. Chem. Soc. , vol.133 , Issue.19 , pp. 7336-7339
    • Sawada, T.1    Gellman, S.H.2
  • 53
    • 84886611019 scopus 로고    scopus 로고
    • Role of Ring-Constrained γ-Amino Acid Residues in α/γ-Peptide Folding: Single-Conformation UV and IR Spectroscopy
    • Kusaka, R.; Zhang, D.; Walsh, P. S.; Gord, J. R.; Fisher, B. F.; Gellman, S. H.; Zwier, T. S. Role of Ring-Constrained γ-Amino Acid Residues in α/γ-Peptide Folding: Single-Conformation UV and IR Spectroscopy J. Chem. Phys. A 2013, 117 (42) 10847-10862
    • (2013) J. Chem. Phys. A , vol.117 , Issue.42 , pp. 10847-10862
    • Kusaka, R.1    Zhang, D.2    Walsh, P.S.3    Gord, J.R.4    Fisher, B.F.5    Gellman, S.H.6    Zwier, T.S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.