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Volumn 259, Issue 3, 1999, Pages 776-789

Mimicry of βII'-turns of proteins in cyclic pentapeptides with one without D-amino acids

Author keywords

Conformation; Cyclic pentapeptide; D amino acid; NMR; Turn

Indexed keywords

ASPARTIC ACID; CYCLO(ASPARTYL PHENYLALANYL LYSYL ALANYL THREONINE); PENTAPEPTIDE; UNCLASSIFIED DRUG;

EID: 0006986790     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00097.x     Document Type: Article
Times cited : (21)

References (51)
  • 1
    • 0001447789 scopus 로고
    • The cyclic peptides: Structure, conformation, and function
    • Neurath, H. & Hill, R.L., eds. Academic, New York
    • 1. Ovchinnikov, Y.A. & Ivannov, V.T. (1982) The cyclic peptides: structure, conformation, and function. In Proteins, 3rd edn, (Neurath, H. & Hill, R.L., eds), pp. 307-642. Academic, New York.
    • (1982) Proteins, 3rd Edn , pp. 307-642
    • Ovchinnikov, Y.A.1    Ivannov, V.T.2
  • 2
    • 0025336463 scopus 로고
    • Emerging approaches in the molecular design of receptor-selective peptide ligands: Conformational. Topographical and dynamic considerations
    • 2. Hruby, V.J., Al-Obeidi, F. & Kazmierski, W. (1990) Emerging approaches in the molecular design of receptor-selective peptide ligands: conformational. topographical and dynamic considerations. Biochem. J. 268, 249-262.
    • (1990) Biochem. J. , vol.268 , pp. 249-262
    • Hruby, V.J.1    Al-Obeidi, F.2    Kazmierski, W.3
  • 3
    • 0026766974 scopus 로고
    • Constrained peptides: Models of bioactive peptides and protein substructures
    • 3. Rizo, J. & Gierasch, L.M. (1992) Constrained peptides: models of bioactive peptides and protein substructures. Ann. Rev. Biochem. 61, 387-418.
    • (1992) Ann. Rev. Biochem. , vol.61 , pp. 387-418
    • Rizo, J.1    Gierasch, L.M.2
  • 4
    • 0027102818 scopus 로고
    • Conformation/activity studies of rationally designed potent anti-adhesive RGD peptides
    • 4. Gurrath, M., Müller, G., Kessler, H., Aumailley, M. & Timpl, R. (1992) Conformation/activity studies of rationally designed potent anti-adhesive RGD peptides. Eur. J. Biochem. 210, 911-921.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 911-921
    • Gurrath, M.1    Müller, G.2    Kessler, H.3    Aumailley, M.4    Timpl, R.5
  • 7
    • 0021844602 scopus 로고
    • β-hairpin families in globular proteins
    • 7. Sibanda, B.L. & Thornton, J.M. (1985) β-hairpin families in globular proteins. Nature 316, 170-176.
    • (1985) Nature , vol.316 , pp. 170-176
    • Sibanda, B.L.1    Thornton, J.M.2
  • 8
    • 0019443447 scopus 로고
    • The anatonomy and taxonomy of protein structure
    • 8. Richardson, J.S. (1981) The anatonomy and taxonomy of protein structure. Adv. Protein Chem. 34, 167-339.
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 12
    • 0342420730 scopus 로고    scopus 로고
    • Comparison of proline and N-methyl norleucine induced conformational equilibria in cyclic pentapeptides
    • 12. Weißhoff, H., Wieprecht, T., Henklein, P., Frömmel, C., Antz, C. & Mügge, C. (1996) Comparison of proline and N-methyl norleucine induced conformational equilibria in cyclic pentapeptides. FEBS Lett. 387, 201-207.
    • (1996) FEBS Lett. , vol.387 , pp. 201-207
    • Weißhoff, H.1    Wieprecht, T.2    Henklein, P.3    Frömmel, C.4    Antz, C.5    Mügge, C.6
  • 13
    • 0027006846 scopus 로고
    • Solution conformations of two flexible cyclic pentapeptides: Cyclo (Gly-Pro-D-Phe-Gly-Ala) and cyclo (Gly-Pro-D-Phe-Gly-Val)
    • 13. Stroup, A.N., Rockwell, A.L. & Gierasch, L.M. (1992) Solution conformations of two flexible cyclic pentapeptides: cyclo (Gly-Pro-D-Phe-Gly-Ala) and cyclo (Gly-Pro-D-Phe-Gly-Val). Biopolymers 32, 1713-1725.
    • (1992) Biopolymers , vol.32 , pp. 1713-1725
    • Stroup, A.N.1    Rockwell, A.L.2    Gierasch, L.M.3
  • 14
    • 0025156939 scopus 로고
    • Cyclic pentapeptides as models for reverse turns: Determination of the equilibrium distribution between type I and type II conformations of Pro-Asn and Pro-Ala β-turns
    • 14. Stradley, S.J., Rizo, J., Bruch, M.D., Stroup. A.N. & Gierasch, L.M. (1990) Cyclic pentapeptides as models for reverse turns: determination of the equilibrium distribution between type I and type II conformations of Pro-Asn and Pro-Ala β-turns. Biopolymers 29, 263-287.
    • (1990) Biopolymers , vol.29 , pp. 263-287
    • Stradley, S.J.1    Rizo, J.2    Bruch, M.D.3    Stroup, A.N.4    Gierasch, L.M.5
  • 15
    • 0025880146 scopus 로고
    • Arg-Gly-Asp constrained within cyclic pentapeptides: Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1
    • 15. Aumailley, M., Gurrath, M., Müller, G., Calvete, J., Timpl, R. & Kessler, H. (1991) Arg-Gly-Asp constrained within cyclic pentapeptides: strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1. FEBS Lett. 291, 50-54.
    • (1991) FEBS Lett. , vol.291 , pp. 50-54
    • Aumailley, M.1    Gurrath, M.2    Müller, G.3    Calvete, J.4    Timpl, R.5    Kessler, H.6
  • 16
    • 0029805817 scopus 로고    scopus 로고
    • Multiple solution conformations of integrin-binding cyclic pentapeptide cyclo (-Ser-D-Leu-Asp-Val-Pro-) - Analysis of the (φ,ψ) space available to cyclic pentapeptides
    • 16. Viles, J.H., Mitchell, J.B.O., Gough, S.L., Doyle, P.M., Harris, C.J., Sadler, P.J. & Thornton, J.M. (1996) Multiple solution conformations of integrin-binding cyclic pentapeptide cyclo (-Ser-D-Leu-Asp-Val-Pro-) - analysis of the (φ,ψ) space available to cyclic pentapeptides. Eur. J. Biochem. 242, 352-362.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 352-362
    • Viles, J.H.1    Mitchell, J.B.O.2    Gough, S.L.3    Doyle, P.M.4    Harris, C.J.5    Sadler, P.J.6    Thornton, J.M.7
  • 17
    • 0028014610 scopus 로고
    • Bioactive peptides: Solid state, solution, and molecular dynamics studies of a cyclolinopeptide A-related cystinyl cyclopentapeptide
    • 17. Rossi, F., Saviano, M., Di Blasio, B., Zanotti, G., Maione, A.M., Tancredi, T. & Pedone, C. (1994) Bioactive peptides: solid state, solution, and molecular dynamics studies of a cyclolinopeptide A-related cystinyl cyclopentapeptide. Biopolymers 34, 273-284.
    • (1994) Biopolymers , vol.34 , pp. 273-284
    • Rossi, F.1    Saviano, M.2    Di Blasio, B.3    Zanotti, G.4    Maione, A.M.5    Tancredi, T.6    Pedone, C.7
  • 18
    • 0029091099 scopus 로고
    • Novel disulfide-constrained pentapeptides as models for β-VIa turns in proteins
    • 18. Weißhoff, H., Frost, K., Brandt, W., Henklein, P., Mügge, C. & Frömmel, C. (1995) Novel disulfide-constrained pentapeptides as models for β-VIa turns in proteins. FEBS Lett. 372, 203-209.
    • (1995) FEBS Lett. , vol.372 , pp. 203-209
    • Weißhoff, H.1    Frost, K.2    Brandt, W.3    Henklein, P.4    Mügge, C.5    Frömmel, C.6
  • 19
    • 0020214401 scopus 로고
    • Unusual intramolecular hydrogen bonding in cycloamanide A, cyclic (L-Pro-L-Val-L-Phe-L-Phe-L-Ala-Gly). A crystal structure analysis
    • 19. Chiang, C.C., Karle, I.L. & Wieland, T. (1982) Unusual intramolecular hydrogen bonding in cycloamanide A, cyclic (L-Pro-L-Val-L-Phe-L-Phe-L-Ala-Gly). A crystal structure analysis. Int. J. Peptide Protein Res. 20, 414-420.
    • (1982) Int. J. Peptide Protein Res. , vol.20 , pp. 414-420
    • Chiang, C.C.1    Karle, I.L.2    Wieland, T.3
  • 20
    • 0014347799 scopus 로고
    • Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units
    • 20. Venkatachalam, C.M. (1968) Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units, Biopolymers 6, 1425-1436.
    • (1968) Biopolymers , vol.6 , pp. 1425-1436
    • Venkatachalam, C.M.1
  • 21
    • 0017709445 scopus 로고
    • β-turns in proteins
    • 21. Chou, P.Y. & Fasman, G.D. (1977) β-turns in proteins. J. Mol. Biol. 115, 135-175.
    • (1977) J. Mol. Biol. , vol.115 , pp. 135-175
    • Chou, P.Y.1    Fasman, G.D.2
  • 22
    • 0009503467 scopus 로고
    • Peptide engineering: Design of biologically active peptides under conformational control
    • The Netherlands, 1989, (Claassen, V. ed.), Elsevier Science, Amsterdam
    • 22. Kessler, H. (1990) Peptide engineering: design of biologically active peptides under conformational control. In Trends in Drug Research (Proceedings of 7th Noordwijkerhout-Camerino Symposium, The Netherlands, 1989), (Claassen, V. ed.), pp. 73-84. Elsevier Science, Amsterdam.
    • (1990) Trends in Drug Research (Proceedings of 7th Noordwijkerhout-camerino Symposium , pp. 73-84
    • Kessler, H.1
  • 23
    • 51249162754 scopus 로고
    • Stereochemical studies on cyclic peptides: Detailed energy minimization studies on hydrogen bonded all-trans cyclic pentapeptide backbones
    • 23. Nagarajaram, H.A. & Ramakrishnan, C. (1995) Stereochemical studies on cyclic peptides: detailed energy minimization studies on hydrogen bonded all-trans cyclic pentapeptide backbones. J. Biosci. 20, 591-611.
    • (1995) J. Biosci. , vol.20 , pp. 591-611
    • Nagarajaram, H.A.1    Ramakrishnan, C.2
  • 24
    • 0022448496 scopus 로고
    • Synthese von cyclischen Pentapepti-danalogen des Thymopoietins. Cyclisierungen mit Carbodiimid und 4-(Dimethylamino) pyridin
    • 24. Kessler, H. & Kutscher, B. (1986) Synthese von cyclischen Pentapepti-danalogen des Thymopoietins. Cyclisierungen mit Carbodiimid und 4-(Dimethylamino) pyridin. Liebigs Ann. Chem. 869-892.
    • (1986) Liebigs Ann. Chem. , pp. 869-892
    • Kessler, H.1    Kutscher, B.2
  • 25
    • 12044258245 scopus 로고
    • 1-Hydroxy-7-azabenzotriazole. An efficient peptide coupling additive
    • 25. Carpino, L.A. (1993) 1-Hydroxy-7-azabenzotriazole. An efficient peptide coupling additive. J. Am. Chem. Soc. 115, 4397-4398.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4397-4398
    • Carpino, L.A.1
  • 26
    • 0030470879 scopus 로고    scopus 로고
    • Cyclization of all-I-pentapeptides by means of 1-hydroxy-7-azabenzotriazole-derived uronium and phosphonium reagents
    • 26. Ehrlich, A., Heyne, H.-U., Winter, R., Beyermann, M., Haber, H., Carpino, L.A. & Bienert, M. (1996) Cyclization of all-I-pentapeptides by means of 1-hydroxy-7-azabenzotriazole-derived uronium and phosphonium reagents. J. Org. Chem. 61, 8831-8838.
    • (1996) J. Org. Chem. , vol.61 , pp. 8831-8838
    • Ehrlich, A.1    Heyne, H.-U.2    Winter, R.3    Beyermann, M.4    Haber, H.5    Carpino, L.A.6    Bienert, M.7
  • 27
    • 0029089390 scopus 로고
    • Cyclic cholecystokinin-analog pentapeptide cyclo (Asp-Trp-Met-Asp-Phe): An unexpected solution conformation
    • 27. Weißhoff, H., Wieprecht, T., Henklein, P., Antz. C. & Mügge, C. (1995) Cyclic cholecystokinin-analog pentapeptide cyclo (Asp-Trp-Met-Asp-Phe): an unexpected solution conformation. Biochem. Biophys. Res. Commun. 213, 506-512.
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 506-512
    • Weißhoff, H.1    Wieprecht, T.2    Henklein, P.3    Antz, C.4    Mügge, C.5
  • 30
    • 0013596756 scopus 로고
    • Bruker Analytische Messtechnik GmbH, FRG
    • 30. AURELIA, Version 941101.3 Bruker Analytische Messtechnik GmbH, FRG (1994).
    • (1994) AURELIA, Version 941101.3
  • 31
    • 0001273885 scopus 로고
    • ROESY relaxation theory
    • 31. Bull, T.E. (1988) ROESY relaxation theory. J. Magn. Reson. 80, 470-481.
    • (1988) J. Magn. Reson. , vol.80 , pp. 470-481
    • Bull, T.E.1
  • 32
    • 0005470885 scopus 로고    scopus 로고
    • Bruker-Franzen Analytik GmbH, FRG
    • 32. WIN-DAISY, Version 4.0 Bruker-Franzen Analytik GmbH, FRG (1997).
    • (1997) WIN-DAISY, Version 4.0
  • 33
    • 0004210285 scopus 로고
    • BIOSYM Technologies Inc., San Diego, CA
    • 33. Insight II, BIOSYM Technologies Inc., San Diego, CA (1995).
    • (1995) Insight II
  • 34
    • 0004283186 scopus 로고
    • Yale University Press, New Haven, CT
    • 34. Brunger, A.T. (1992) X-PLOR 3.1 Yale University Press, New Haven, CT.
    • (1992) X-PLOR 3.1
    • Brunger, A.T.1
  • 35
    • 0029931671 scopus 로고    scopus 로고
    • Stereochemical requirements for β-hairpin formation: Model studies with four-residue peptides and depsipeptides
    • 35. Haque, T.S., Little, J.C. & Gellman, S.H. (1996) Stereochemical requirements for β-hairpin formation: model studies with four-residue peptides and depsipeptides, J. Am. Chem. Soc. 118, 6975-6985.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6975-6985
    • Haque, T.S.1    Little, J.C.2    Gellman, S.H.3
  • 39
    • 84985733652 scopus 로고
    • Proton NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • 39. Bundi, A. & Wüthrich, K. (1979) Proton NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH. Biopolymers 18, 285-297.
    • (1979) Biopolymers , vol.18 , pp. 285-297
    • Bundi, A.1    Wüthrich, K.2
  • 40
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secundary structure through NMR spectroscopy
    • 40. Wishart, D.S., Sykes, B.D. & Richards, F.M. (1992) The chemical shift index: a fast and simple method for the assignment of protein secundary structure through NMR spectroscopy. Biochemistry 31, 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 41
    • 0000021544 scopus 로고
    • Ein chemischer weg zu neuen proteinen - Templat-assoziene synthetische proteine (TASP)
    • 41. Mutter, M. & Vuilleumier, S. (1989) Ein chemischer Weg zu neuen Proteinen - templat-assoziene synthetische Proteine (TASP). Angew. Chem. 101, 551-571.
    • (1989) Angew. Chem. , vol.101 , pp. 551-571
    • Mutter, M.1    Vuilleumier, S.2
  • 42
    • 0024279235 scopus 로고
    • Analysis and prediction of different types of β-turns in proteins
    • 42. Wilmot, C.M. & Thornton, J.M. (1988) Analysis and prediction of different types of β-turns in proteins. J. Mol. Biol. 203, 221-232.
    • (1988) J. Mol. Biol. , vol.203 , pp. 221-232
    • Wilmot, C.M.1    Thornton, J.M.2
  • 43
    • 0000291574 scopus 로고
    • Mirror image reverse turns promote β-hairpin formation
    • 43. Haque. T.S., Little, J.C. & Gellman, S.H. (1994) Mirror image reverse turns promote β-hairpin formation. J. Am. Chem. Soc. 116, 4105-4106.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 4105-4106
    • Haque, T.S.1    Little, J.C.2    Gellman, S.H.3
  • 44
    • 0029891313 scopus 로고    scopus 로고
    • De novo design and structural analysis of a model β-hairpin peptide system
    • 44. Ramirez-Alvarado, M., Blanco, F.J. & Serrano, L. (1996) De novo design and structural analysis of a model β-hairpin peptide system. Nature Structural Biology 3. 604-612.
    • (1996) Nature Structural Biology , vol.3 , pp. 604-612
    • Ramirez-Alvarado, M.1    Blanco, F.J.2    Serrano, L.3
  • 45
    • 0346837918 scopus 로고    scopus 로고
    • β-hairpin nucleation by Pro-Gly β-turns. Comparison of D-Pro-Gly and L-Pro-Gly sequences in an apolar octapeptide
    • 45. Raghothama, S.R., Awasthi, S.K. & Balaram, P. (1998) β-hairpin nucleation by Pro-Gly β-turns. Comparison of D-Pro-Gly and L-Pro-Gly sequences in an apolar octapeptide. J. Chem. Soc., Perkin Trans. 2, 137-143.
    • (1998) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 137-143
    • Raghothama, S.R.1    Awasthi, S.K.2    Balaram, P.3
  • 47
    • 0028877683 scopus 로고
    • Duodenase, a new serine protease of unusual specificity from bovine duodenal mucosa-primary structure of the enzyme
    • 47. Zamolodchikova, T.S., Vorotyntseva, T.I., Nazimov, I.V. & Grishina, G.A. (1995) Duodenase, a new serine protease of unusual specificity from bovine duodenal mucosa-primary structure of the enzyme. Eur. J. Biochem. 227 (3), 873-879.
    • (1995) Eur. J. Biochem. , vol.227 , Issue.3 , pp. 873-879
    • Zamolodchikova, T.S.1    Vorotyntseva, T.I.2    Nazimov, I.V.3    Grishina, G.A.4
  • 48
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • 48. Pierschbacher, M.D. & Ruoslathi, E. (1984) Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309, 30-33.
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslathi, E.2
  • 49
    • 0025777183 scopus 로고
    • The minimal essential sequence for a major cell type-specific adhesion site (CSI) within the alternatively spliced type III connecting segment domain of fibronectin is leucine-aspartic acid-valine
    • 49. Komoriya, A., Green, L.J., Mervic, M., Yamada, S.S., Yamada, K.M. & Humphries, M.J. (1991) The minimal essential sequence for a major cell type-specific adhesion site (CSI) within the alternatively spliced type III connecting segment domain of fibronectin is leucine-aspartic acid-valine. J. Biol. Chem. 266, 15075-15079.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15075-15079
    • Komoriya, A.1    Green, L.J.2    Mervic, M.3    Yamada, S.S.4    Yamada, K.M.5    Humphries, M.J.6
  • 50
    • 0020688764 scopus 로고
    • Cleavage at aspartic acid
    • 50. Inglis, A.S. (1983) Cleavage at aspartic acid. Methods Enzymology 91, 324-332.
    • (1983) Methods Enzymology , vol.91 , pp. 324-332
    • Inglis, A.S.1


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