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Volumn 118, Issue 28, 2014, Pages 8246-8256

Mimicking the first turn of an α-helix with an unnatural backbone: Conformation-specific IR and UV spectroscopy of cyclically constrained β/γ-peptides

Author keywords

[No Author keywords available]

Indexed keywords

AMIDES; CONFORMATIONS; INFRARED SPECTROSCOPY; ISOMERS; PEPTIDES; ULTRAVIOLET SPECTROSCOPY;

EID: 84904544686     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp5015884     Document Type: Article
Times cited : (22)

References (32)
  • 1
    • 84867868384 scopus 로고    scopus 로고
    • Carbohydrate-derived conformationally restricted bicyclic dipeptides as potential hetero foldamer building blocks
    • Ramesh, V. V. E.; Puranik, V. G.; Sanjayan, G. J. Carbohydrate-derived conformationally restricted bicyclic dipeptides as potential hetero foldamer building blocks Tetrahedron: Asymmetry 2012, 23, 1400-1404
    • (2012) Tetrahedron: Asymmetry , vol.23 , pp. 1400-1404
    • Ramesh, V.V.E.1    Puranik, V.G.2    Sanjayan, G.J.3
  • 2
    • 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, 6574-6590
    • (2009) J. Am. Chem. Soc. , vol.131 , 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
  • 3
    • 0032906918 scopus 로고    scopus 로고
    • Hydrogen bonds in molecular assemblies of natural, synthetic and "designer" peptides
    • Karle, I. L. Hydrogen bonds in molecular assemblies of natural, synthetic and "designer" peptides J. Mol. Struct. 1999, 474, 103-112
    • (1999) J. Mol. Struct. , vol.474 , pp. 103-112
    • Karle, I.L.1
  • 4
    • 57149097169 scopus 로고    scopus 로고
    • β-Peptidic Peptidomimetics
    • Seebach, D.; Gardiner, J. β-Peptidic Peptidomimetics Acc. Chem. Res. 2008, 41, 1366-1375
    • (2008) Acc. Chem. Res. , vol.41 , pp. 1366-1375
    • Seebach, D.1    Gardiner, J.2
  • 5
    • 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
    • (2008) Acc. Chem. Res. , vol.41 , pp. 1399-1408
    • Horne, W.S.1    Gellman, S.H.2
  • 6
    • 80052325324 scopus 로고    scopus 로고
    • Foldamers Containing γ-Amino Acid Residues or Their Analogues: Structural Features and Applications
    • Bouillere, F.; Thetiot-Laurent, S.; Kouklovsky, C.; Alezra, V. Foldamers Containing γ-Amino Acid Residues or Their Analogues: Structural Features and Applications Amino Acids 2011, 41, 687-707
    • (2011) Amino Acids , vol.41 , pp. 687-707
    • Bouillere, F.1    Thetiot-Laurent, S.2    Kouklovsky, C.3    Alezra, V.4
  • 7
    • 0030833324 scopus 로고    scopus 로고
    • ω-Amino Acids in Peptide Design. Crystal Structures and Solution Conformations of Peptide Helices Containing a β-Alanyl-γ-Aminobutyryl Segment
    • Karle, I. L.; Pramanik, A.; Banerjee, A.; Bhattacharjya, S.; Balaram, P. ω-Amino Acids in Peptide Design. Crystal Structures and Solution Conformations of Peptide Helices Containing a β-Alanyl-γ-Aminobutyryl Segment J. Am. Chem. Soc. 1997, 119, 9087-9095
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 9087-9095
    • Karle, I.L.1    Pramanik, A.2    Banerjee, A.3    Bhattacharjya, S.4    Balaram, P.5
  • 8
    • 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.; Gunther, 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
    • (2006) J. Org. Chem. , vol.71 , pp. 1200-1208
    • Baldauf, C.1    Gunther, R.2    Hofmann, H.J.3
  • 10
    • 84897013072 scopus 로고    scopus 로고
    • An Unusual Interstrand H-Bond Stabilizes the Heteroassembly of Helical αβγ-Chimeras with Natural Peptides
    • Nyakatura, E. K.; Araghi, R. R.; Mortier, J.; Wieczorek, S.; Baldauf, C.; Wolber, G.; Koksch, B. An Unusual Interstrand H-Bond Stabilizes the Heteroassembly of Helical αβγ-Chimeras with Natural Peptides ACS Chem. Biol. 2013, 9, 613-616
    • (2013) ACS Chem. Biol. , vol.9 , pp. 613-616
    • Nyakatura, E.K.1    Araghi, R.R.2    Mortier, J.3    Wieczorek, S.4    Baldauf, C.5    Wolber, G.6    Koksch, B.7
  • 11
    • 77953314514 scopus 로고    scopus 로고
    • Helix Formation in Preorganized β/γ-Peptide Foldamers: Hydrogen-Bond Analogy to the α-Helix without α-Amino Acid Residues
    • Guo, L.; Almeida, A. M.; Zhang, W.; Reidenbach, A. G.; Choi, S. H.; Guzei, I. A.; Gellman, S. H. Helix Formation in Preorganized β/γ-Peptide Foldamers: Hydrogen-Bond Analogy to the α-Helix without α-Amino Acid Residues J. Am. Chem. Soc. 2010, 132, 7868-7869
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 7868-7869
    • Guo, L.1    Almeida, A.M.2    Zhang, W.3    Reidenbach, A.G.4    Choi, S.H.5    Guzei, I.A.6    Gellman, S.H.7
  • 12
    • 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, 1628-1639
    • (2009) Acc. Chem. Res. , vol.42 , pp. 1628-1639
    • Vasudev, P.G.1    Chatterjee, S.2    Shamala, N.3    Balaram, P.4
  • 15
    • 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, 209-226
    • (2011) Faraday Discuss. , vol.150 , 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
  • 17
    • 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
    • 094301
    • Buchanan, E. G.; James, W. H., III; Choi, S. H.; Guo, L.; Gellman, S. H.; Müller, 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 094301
    • (2012) J. Chem. Phys. , vol.137
    • Buchanan, E.G.1    James III, W.H.2    Choi, S.H.3    Guo, L.4    Gellman, S.H.5    Müller, C.W.6    Zwier, T.S.7
  • 18
    • 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. Phys. Chem. A 2010, 114, 1581-1591
    • (2010) J. Phys. Chem. A , vol.114 , pp. 1581-1591
    • James III, W.H.1    Baquero, E.E.2    Choi, S.H.3    Gellman, S.H.4    Zwier, T.S.5
  • 19
    • 84886634658 scopus 로고    scopus 로고
    • Cyclic Constraints on Conformational Flexibility in γ-Peptides: Conformation Specific IR and UV Spectroscopy
    • Walsh, P. S.; Kusaka, R.; Buchanan, E. G.; James, W. H., III; Fisher, B. F.; Gellman, S. H.; Zwier, T. S. Cyclic Constraints on Conformational Flexibility in γ-Peptides: Conformation Specific IR and UV Spectroscopy J. Phys. Chem. A 2013, 117, 12350-12362
    • (2013) J. Phys. Chem. A , vol.117 , pp. 12350-12362
    • Walsh, P.S.1    Kusaka, R.2    Buchanan, E.G.3    James III, W.H.4    Fisher, B.F.5    Gellman, S.H.6    Zwier, T.S.7
  • 20
    • 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. Phys. Chem. A 2011, 115, 11960-11970
    • (2011) J. Phys. Chem. A , vol.115 , pp. 11960-11970
    • James III, W.H.1    Buchanan, E.G.2    Guo, L.3    Gellman, S.H.4    Zwier, T.S.5
  • 21
    • 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. Phys. Chem. A 2013, 117, 10847-10862
    • (2013) J. Phys. Chem. A , vol.117 , 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
  • 22
    • 43949090855 scopus 로고    scopus 로고
    • Crystallographic characterization of helical secondary structures in α/β-peptides with 1:1 residue alternation
    • Choi, S. H.; Guzei, I. A.; Spencer, L. C.; Gellman, S. H. Crystallographic characterization of helical secondary structures in α/β-peptides with 1:1 residue alternation J. Am. Chem. Soc. 2008, 130, 6544-6550
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 6544-6550
    • Choi, S.H.1    Guzei, I.A.2    Spencer, L.C.3    Gellman, S.H.4
  • 23
    • 67749103828 scopus 로고    scopus 로고
    • Crystallographic Characterization of Helical Secondary Structures in 2:1 and 1:2 α/β-Peptides
    • Choi, S. H.; Guzei, I. A.; Spencer, L. C.; Gellman, S. H. Crystallographic Characterization of Helical Secondary Structures in 2:1 and 1:2 α/β-Peptides J. Am. Chem. Soc. 2009, 131, 2917-2924
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2917-2924
    • Choi, S.H.1    Guzei, I.A.2    Spencer, L.C.3    Gellman, S.H.4
  • 24
    • 77957302949 scopus 로고    scopus 로고
    • Crystallographic Characterization of 12-Helical Secondary Structure in β-Peptides Containing Side Chain Groups
    • Choi, S. H.; Guzei, I. A.; Spencer, L. C.; Gellman, S. H. Crystallographic Characterization of 12-Helical Secondary Structure in β-Peptides Containing Side Chain Groups J. Am. Chem. Soc. 2010, 132, 13879-13885
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 13879-13885
    • Choi, S.H.1    Guzei, I.A.2    Spencer, L.C.3    Gellman, S.H.4
  • 25
    • 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. G.; 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, 16018-16020
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 16018-16020
    • Guo, L.1    Chi, Y.G.2    Almeida, A.M.3    Guzei, I.A.4    Parker, B.K.5    Gellman, S.H.6
  • 28
    • 33847181474 scopus 로고
    • Time-of-Flight Mass Spectrometer with Improved Resolution
    • Wiley, W. C.; McLaren, I. H. Time-of-Flight Mass Spectrometer with Improved Resolution Rev. Sci. Instrum. 1955, 26, 1150-1157
    • (1955) Rev. Sci. Instrum. , vol.26 , pp. 1150-1157
    • Wiley, W.C.1    McLaren, I.H.2
  • 31
    • 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, 289-300
    • (2007) J. Chem. Theory Comput. , vol.3 , pp. 289-300
    • Zhao, Y.1    Truhlar, D.G.2


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