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Volumn 91, Issue 9, 2006, Pages 3425-3435

Thermodynamic stability of β-peptide helices and the role of cyclic residues

Author keywords

[No Author keywords available]

Indexed keywords

BETA PEPTIDE; PEPTIDE; UNCLASSIFIED DRUG;

EID: 33751206868     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.084491     Document Type: Article
Times cited : (51)

References (46)
  • 1
    • 0542421525 scopus 로고    scopus 로고
    • Foldamers: A manifesto
    • Gellman, S. H. 1998. Foldamers: a manifesto. Acc. Chem. Res. 31:173-180.
    • (1998) Acc. Chem. Res. , vol.31 , pp. 173-180
    • Gellman, S.H.1
  • 3
    • 58149184505 scopus 로고    scopus 로고
    • Aromatic oligoamide foldamers
    • Huc, I. 2004. Aromatic oligoamide foldamers. Eur. J. Org. Chem. 1:17-29.
    • (2004) Eur. J. Org. Chem. , vol.1 , pp. 17-29
    • Huc, I.1
  • 4
    • 0035471135 scopus 로고    scopus 로고
    • β-peptides: From structure to function
    • Cheng, R. P., S. H. Gellman, and W. F. DeGrado. 2001. β-peptides: from structure to function. Chem. Rev. 101:3219-3232.
    • (2001) Chem. Rev. , vol.101 , pp. 3219-3232
    • Cheng, R.P.1    Gellman, S.H.2    DeGrado, W.F.3
  • 5
    • 9444226868 scopus 로고    scopus 로고
    • The world of β- and γ-peptides comprised of homologated proteinogenic amino acids and other components
    • Seebach, D., A. K. Beck, and D. J. Bierbaum. 2004. The world of β- and γ-peptides comprised of homologated proteinogenic amino acids and other components. Chem. Biodivers. 1:1111-1239.
    • (2004) Chem. Biodivers , vol.1 , pp. 1111-1239
    • Seebach, D.1    Beck, A.K.2    Bierbaum, D.J.3
  • 6
    • 0033577324 scopus 로고    scopus 로고
    • Formation of short, stable helices in aqueous solution by β-amino acid hexamers
    • Appella, D. H., J. J. J. Barchi, S. R. Durell, and S. H. Gellman. 1999. Formation of short, stable helices in aqueous solution by β-amino acid hexamers. J. Am. Chem. Soc. 121:2309-2310.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2309-2310
    • Appella, D.H.1    Barchi, J.J.J.2    Durell, S.R.3    Gellman, S.H.4
  • 7
    • 0034679022 scopus 로고    scopus 로고
    • 12-Helix formation in aqueous solution with short β-peptides containing pyrrolidine-based residues
    • Wang, X., J. F. Espinosa, and S. H. Gellman. 2000. 12-helix formation in aqueous solution with short β-peptides containing pyrrolidine-based residues. J. Am. Chem. Soc. 122:4821-4822.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 4821-4822
    • Wang, X.1    Espinosa, J.F.2    Gellman, S.H.3
  • 8
    • 0034800435 scopus 로고    scopus 로고
    • Diversity in short β-peptide 12-helices: High resolution structural analysis in aqueous solution of a hexamer containing sulfonylated pyrrolidine residues
    • Lee, H. S., F. A. Syud, X. Wang, and S. H. Gellman. 2001. Diversity in short β-peptide 12-helices: high resolution structural analysis in aqueous solution of a hexamer containing sulfonylated pyrrolidine residues. J. Am. Chem. Soc. 123:7721-7722.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7721-7722
    • Lee, H.S.1    Syud, F.A.2    Wang, X.3    Gellman, S.H.4
  • 10
    • 0037959630 scopus 로고    scopus 로고
    • Environment-independent 14-helix formation in short β-peptides: Striking a balance between shape control and functional diversity
    • Raguse, T. L., J. R. Lai, and S. H. Gellman. 2003. Environment- independent 14-helix formation in short β-peptides: striking a balance between shape control and functional diversity. J. Am. Chem. Soc. 125:5592-5593.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5592-5593
    • Raguse, T.L.1    Lai, J.R.2    Gellman, S.H.3
  • 13
    • 0032881267 scopus 로고    scopus 로고
    • Beta-peptides as inhibitors of small-intestinal cholesterol and fat absorption
    • Werder, M., S. Abele, and D. Seebach. 1999. Beta-peptides as inhibitors of small-intestinal cholesterol and fat absorption. Helv. Chim. Acta. 82:1774-1783.
    • (1999) Helv. Chim. Acta , vol.82 , pp. 1774-1783
    • Werder, M.1    Abele, S.2    Seebach, D.3
  • 14
    • 0033616105 scopus 로고    scopus 로고
    • De novo design of antibacterial β-peptides
    • Hamuro, Y., J. P. Schneider, and W. L. DeGrado. 1999. De novo design of antibacterial β-peptides. J. Am. Chem. Soc. 121:12200-12201.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 12200-12201
    • Hamuro, Y.1    Schneider, J.P.2    DeGrado, W.L.3
  • 15
  • 16
    • 27144443340 scopus 로고    scopus 로고
    • A rapid library screening for tailoring β-peptide structure and function
    • Kritzer, J. A., N. W. Luedtke, E. A. Harker, and A. Schepartz. 2005. A rapid library screening for tailoring β-peptide structure and function. J. Am. Chem. Soc. 127:14584-14585.
    • (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
  • 18
    • 33646357930 scopus 로고    scopus 로고
    • Rational development of β-peptide inhibitors of human cytomegalovirus entry
    • In press
    • English, E. P., R. S. Chumanov, S. H. Gellman, and T. Compton. 2006. Rational development of β-peptide inhibitors of human cytomegalovirus entry. J. Biol. Chem. In press.
    • (2006) J. Biol. Chem.
    • English, E.P.1    Chumanov, R.S.2    Gellman, S.H.3    Compton, T.4
  • 19
    • 0032583445 scopus 로고    scopus 로고
    • Theoretical studies of β-peptide models
    • Wu, Y.-D., and D.-P. Wang. 1998. Theoretical studies of β-peptide models. J. Am. Chem. Soc. 120:13485-13493.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 13485-13493
    • Wu, Y.-D.1    Wang, D.-P.2
  • 20
    • 0033557181 scopus 로고    scopus 로고
    • Folding-unfolding thermodynamics of a β-heptapeptide from equilibrium simulations
    • Daura, X., W. F. van Gunsteren, and A. E. Mark. 1999. Folding-unfolding thermodynamics of a β-heptapeptide from equilibrium simulations. Proteins Struct. Funct. Genet. 34:269-280.
    • (1999) Proteins Struct. Funct. Genet. , vol.34 , pp. 269-280
    • Daura, X.1    Van Gunsteren, W.F.2    Mark, A.E.3
  • 21
    • 0034806777 scopus 로고    scopus 로고
    • The β-peptide hairpin in solution: Conformational study of a β-hexapeptide in methanol by NMR spectroscopy and MD simulation
    • Daura, X., K. Gademann, H. Schafer, B. Jaun, D. Seebach, and W. F. van Gunsteren. 2001. The β-peptide hairpin in solution: conformational study of a β-hexapeptide in methanol by NMR spectroscopy and MD simulation. J. Am. Chem. Soc. 123:2393-2404.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2393-2404
    • Daura, X.1    Gademann, K.2    Schafer, H.3    Jaun, B.4    Seebach, D.5    Van Gunsteren, W.F.6
  • 22
    • 0035314075 scopus 로고    scopus 로고
    • Entropy calculations on a reversibly folding peptide: Changes in solute free energy cannot explain folding behavior
    • Schafer, H., X. Daura, A. E. Mark, and W. F. van Gunsteren. 2001. Entropy calculations on a reversibly folding peptide: changes in solute free energy cannot explain folding behavior. Proteins Struct. Funct. Genet. 43:45-56.
    • (2001) Proteins Struct. Funct. Genet. , vol.43 , pp. 45-56
    • Schafer, H.1    Daura, X.2    Mark, A.E.3    Van Gunsteren, W.F.4
  • 23
    • 8644241573 scopus 로고    scopus 로고
    • Do valine side chains have an influence of folding behavior of β-substituted β-peptides?
    • Glattli, A., D. Seebach, and W. F. van Gunsteren. 2004. Do valine side chains have an influence of folding behavior of β-substituted β-peptides? Helv. Chim. Acta. 87:2487-2506.
    • (2004) Helv. Chim. Acta , vol.87 , pp. 2487-2506
    • Glattli, A.1    Seebach, D.2    Van Gunsteren, W.F.3
  • 25
    • 0035859447 scopus 로고    scopus 로고
    • Searching for periodic structures in β-peptides
    • Gunther, R., and H.-J. Hofmann. 2001. Searching for periodic structures in β-peptides. J. Phys. Chem. B. 105:5559-5567.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 5559-5567
    • Gunther, R.1    Hofmann, H.-J.2
  • 26
    • 0036338702 scopus 로고    scopus 로고
    • Theoretical prediction of substituent effects on the intrinsic folding properties of β-peptides
    • Gunther, R., and H.-J. Hofmann. 2002. Theoretical prediction of substituent effects on the intrinsic folding properties of β-peptides. Helv. Chim. Acta. 85:2149-2168.
    • (2002) Helv. Chim. Acta , vol.85 , pp. 2149-2168
    • Gunther, R.1    Hofmann, H.-J.2
  • 27
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • Jorgensen, W. L., D. S. Maxwell, and J. Tirado-Rives. 1996. Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J. Am. Chem. Soc. 118:11225-11236.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 28
    • 0035889784 scopus 로고    scopus 로고
    • Efficient exploration of conformational space using the stochastic search method: Application to β-peptide oligomers
    • Chandrasekhar, J., M. Saunders, and W. L. Jorgensen. 2001. Efficient exploration of conformational space using the stochastic search method: application to β-peptide oligomers. J. Comput. Chem. 22:1646-1654.
    • (2001) J. Comput. Chem. , vol.22 , pp. 1646-1654
    • Chandrasekhar, J.1    Saunders, M.2    Jorgensen, W.L.3
  • 31
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transition in single titin modules characterized with laser tweezers
    • Kellermayer, M. S. Z., S. B. Smith, H. L. Granzier, and C. Bustamante. 1997. Folding-unfolding transition in single titin modules characterized with laser tweezers. Science. 276:1112-1116.
    • (1997) Science , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.Z.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 33
    • 0030461803 scopus 로고    scopus 로고
    • β-peptide foldamers: Robust helix formation in a new family of β-amino acid oligomers
    • Appella, D. H., L. A. Christianson, I. L. Karle, D. R. Powell, and S. H. Gellman. 1996. β-peptide foldamers: robust helix formation in a new family of β-amino acid oligomers. J. Am. Chem. Soc. 124:13071-13072.
    • (1996) J. Am. Chem. Soc. , vol.124 , pp. 13071-13072
    • Appella, D.H.1    Christianson, L.A.2    Karle, I.L.3    Powell, D.R.4    Gellman, S.H.5
  • 34
    • 0033532930 scopus 로고    scopus 로고
    • Synthesis and characterization of trans-2-aminocyclohexanecarboxylic acid oligomers: An unnatural helical secondary structure and implications for β-peptide tertiary structure
    • Appella, D. H., L. A. Christianson, I. L. Karle, D. R. Powell, and S. H. Gellman. 1999. Synthesis and characterization of trans-2- aminocyclohexanecarboxylic acid oligomers: an unnatural helical secondary structure and implications for β-peptide tertiary structure. J. Am. Chem. Soc. 121:6206-6212.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 6206-6212
    • Appella, D.H.1    Christianson, L.A.2    Karle, I.L.3    Powell, D.R.4    Gellman, S.H.5
  • 38
    • 0036114441 scopus 로고    scopus 로고
    • Solvation model dependency of helix-coil transition in polyalanine
    • Peng, Y., and U. H. E. Hansmann. 2002. Solvation model dependency of helix-coil transition in polyalanine. Biophys. J. 82:3269-3276.
    • (2002) Biophys. J. , vol.82 , pp. 3269-3276
    • Peng, Y.1    Hansmann, U.H.E.2
  • 39
    • 0036138028 scopus 로고    scopus 로고
    • Evaluation of a fast implicit solvent model for molecular dynamics simulations
    • Ferrara, P., J. Apostolakiz, and A. Caflisch. 2002. Evaluation of a fast implicit solvent model for molecular dynamics simulations. Proteins Struct. Funct. Genet. 46:24-33.
    • (2002) Proteins Struct. Funct. Genet. , vol.46 , pp. 24-33
    • Ferrara, P.1    Apostolakiz, J.2    Caflisch, A.3
  • 40
    • 0000026966 scopus 로고    scopus 로고
    • Explicit reversible integrators for extended systems dynamics
    • Martyna, G. J. 1996. Explicit reversible integrators for extended systems dynamics. Mol. Phys. 87:1117-1157.
    • (1996) Mol. Phys. , vol.87 , pp. 1117-1157
    • Martyna, G.J.1
  • 41
    • 0037159430 scopus 로고    scopus 로고
    • Potential of mean force between a spherical particle suspended in a nematic liquid crystal and a substrate
    • Kim, E. B., R. Faller, Q. Yan, N. L. Abbott, and J. J. de Pablo. 2002. Potential of mean force between a spherical particle suspended in a nematic liquid crystal and a substrate. J. Chem. Phys. 117:7781-7787.
    • (2002) J. Chem. Phys. , vol.117 , pp. 7781-7787
    • Kim, E.B.1    Faller, R.2    Yan, Q.3    Abbott, N.L.4    De Pablo, J.J.5
  • 42
    • 1942535023 scopus 로고    scopus 로고
    • Molecular simulation of the reversible mechanical unfolding of proteins
    • Rathore, N., Q. Yan, and J. J. de Pablo. 2004. Molecular simulation of the reversible mechanical unfolding of proteins. J. Chem. Phys. 120:5781-5788.
    • (2004) J. Chem. Phys. , vol.120 , pp. 5781-5788
    • Rathore, N.1    Yan, Q.2    De Pablo, J.J.3
  • 43
    • 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 towards pepsin
    • Seebach, D., M. Overhand, F. N. M. Kuhnle, B. Martinoni, L. Oberer, U. Hommel, and H. Widmer. 1996. 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 towards pepsin. Helv. Chim. Acta. 79:913-941.
    • (1996) Helv. Chim. Acta , vol.79 , pp. 913-941
    • Seebach, D.1    Overhand, M.2    Kuhnle, F.N.M.3    Martinoni, B.4    Oberer, L.5    Hommel, U.6    Widmer, H.7
  • 44
    • 0030785114 scopus 로고    scopus 로고
    • β-peptides: A surprise at every turn
    • Seebach, D., and J. L. Matthews. 1997. β-peptides: a surprise at every turn. Chem. Commun. 2015-2022.
    • (1997) Chem. Commun. , pp. 2015-2022
    • Seebach, D.1    Matthews, J.L.2
  • 45
    • 0033532930 scopus 로고    scopus 로고
    • Synthesis and structural characterization of helix-forming β-peptides: Trans-2-aminocyclopentanecarboxylic acid oligomers
    • Appella, D. H., L. A. Christianson, D. A. Klein, M. R. Richards, D. R. Powell, and S. H. Gellman. 1999. Synthesis and structural characterization of helix-forming β-peptides: trans-2-aminocyclopentanecarboxylic acid oligomers. J. Am. Chem. Soc. 121:6206-6212.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 6206-6212
    • Appella, D.H.1    Christianson, L.A.2    Klein, D.A.3    Richards, M.R.4    Powell, D.R.5    Gellman, S.H.6
  • 46
    • 0001529568 scopus 로고    scopus 로고
    • Theoretical and experimental circular dichroic spectra of the novel helical foldamer poly[(1r,2r)-trans-2-aminocyclopentanecarboxylic acid]
    • Applequist, J., K. A. Bode, D. H. Apella, L. A. Christianson, and S. H. Gellman. 1998. Theoretical and experimental circular dichroic spectra of the novel helical foldamer poly[(1r,2r)-trans-2-aminocyclopentanecarboxylic acid]. J. Am. Chem. Soc. 120:4891-4892.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4891-4892
    • Applequist, J.1    Bode, K.A.2    Apella, D.H.3    Christianson, L.A.4    Gellman, S.H.5


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