Rational designing of bioactive peptides

Nutraceutical Proteins and Peptides in Health and Disease

Volumn , Issue , 2005, Pages 565-582

  Nakai, Shuryo ^a   Alizadeh Pasdar, Nooshin ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

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[No Author keywords available]

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EID: 85122909138     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter

References (37)

1. A.L. Parrill, M.R. Reddy (Eds.). Rational Drug Design: Novel Methodology and Practical Application. ACS Symposium Series 719. Washington, DC: American Chemical Society, 1999.
2. A.J. Stuper, W.E. Brugger, P.C. Jurs (Eds.). Computer Assisted Studies of Chemical Structure and Biological Function. New York: John Wiley & Sons, 1979.
3. S. Nakai, J. Dou, K.V. Lo, C.H. Scaman. Optimization of site-directed mutagenesis I. New random-centroid optimization for Windows useful in research and development. J. Agric. Food Chem., 46: 1642-1654, 1998.
4. S. Nakai, J. Dou, S. Nakamura, C.H. Scaman. Optimization of site-directed mutagenesis. II. Application of random-centroid optimization to one-site mutation of B. stearothermophilus neutral protease to improve thermostability. J. Agric. Food Chem., 46: 1655-1661, 1998.
5. M. Ogawa, S. Nakamura, C.H. Scaman, H. Jing, D. Kitts, J. Dou, S. Nakai. Enhancement of proteinase inhibitory activity of recombinant human cystatin C using random-centroid optimization. Biochim. Biophys. Acta, 1599: 115-124, 2002.
6. S. Nakai, M. Ogawa, S. Nakamura, J. Dou, K. Funane. A computer-aided strategy for structure-function relation study of food protein using unsupervised data mining. Int. J. Food Prop., 6: 25-47, 2003.
7. S. Nakai, J.C.K. Chan, E.C.Y. Li-Chan, J. Dou, M. Ogawa. Homology similarity analysis of sequence of lactoferricin and its derivatives. J. Agric. Food Chem., 51: 1215-1223, 2003.
8. Pattern similarity analysis based on side-chain properties in searching for functional motifs in protein sequences. I, Lysozyme families and II. Cystatine pro-teinase inhibiton by cystatins. These two articles were combined and published as shown in Reference 9.
9. S. Nakai, E.C.Y. Li-Chan, J. Dou. Pattern similarity study of functional sites in protein sequences: lysozymes and cystatins. BMC Biochem., 9: pp. 1-17 at www.biomedcentral.com/1471-2091/6/9.
10. M.D. Schmidt. Structural proteomics: the potential of high-throughput structure determination. Trends Microbiol., 10: S27-S31, 2002.
11. S. Nakai. Modelling protein behaviour. In: R. Yada (Ed). Protein in Food Processing. Cambridge, UK: Woodhead Publishing, 2004, chapter 11. 245-269.
12. C. Hansch, D. Hoekman, A. Leo, D. Weininger, D. Selassie. Chem-Bioinformatics: comparative QSAR at the interface between chemistry and biology. Chem. Rev., 102: 783-812, 2002.
13. T.W. Schultz, M.T.D. Cronin, J.D. Walker, A.O. Aptula. QSARs in toxicology: a historical perspective. J. Mol. Struct. (Theochem.), 622: 1-22, 2003.
14. C. Hansch, A. Leo, E. Hoekman. Exploring QSAR. Hydrophobic, Electronic, and Steric Constants. Washington, DC: American Chemical Society, 1995. Oxford University Press USA, New York, ISBN 0-8412-2991-0.
15. S. Hellberg, M. Sjöström, B. Skagerberg, S. Rold. Peptide quantitative structure-activity relationships, a multivariate approach. J. Med. Chem., 30: 1126-1135, 1987.
16. M.B. Strøm, Ø. Rekdal, W. Stensen, J.S. Svendsen. Increased antibacterial activity of 15-residue murine lactoferricin derivatives. J. Pept. Res., 57: 127-139, 2001.
17. S. Wold, M. Sjöström, L. Eriksson. PLS-regression: a basic of chemometrics. Chemom. Intel. Syst., 58: 109-130, 2001.
18. F.R. Burden, D.A. Winkler. A quantitative structure-activity relationships model for the active toxicity of substituted benzenes to Tetrahymena pyriformis using Bayesian-regulated neural networks. Chem. Res. Toxicol., 13: 436-440, 2000.
19. G.A. Bakken, P.C. Jurs. QSARs for 6-azasteroids as inhibitors of human type 1 5α-reductase: prediction of binding affinity and selectivity relative to 3-BHSD. J. Chem. Inf. Comput, 41: 1255-1265, 2001.
20. M.T.D. Cronin, T.W. Schultz. Development of quantitative structure-activity relationships for the toxicity of aromatic compounds to Tetrahymena pyriformis: comparative assessment of the methodologies. Chem. Res. Toxicol, 14: 1284-1295, 2001.
21. D. Michalovich, J. Overington, R. Fagan. Protein sequence analysis in silico: application of structure-based bioinformatics to genomic initiatives. Curr. Opin. Pharmacol., 2: 574-580, 2002.
22. A. Giuliani, R. Benigni, J.P. Zbilut, C.L. Webber Jr, P. Sirabella, A. Colosimo. Nonlinear signal analysis methods in the elucidation of protein sequence-structure relationships. Chem. Rev., 102: 1471-1291, 2002.
23. R. Buttimor, D. Rousseau, A. Paulson. Pattern similarity analysis of amino acid sequences for peptide emulsification. J. Agric. Food Chem., 52: 927-934, 2004.
24. M. Saito, M. Ogasawara, K. Chikuni, M. Simizu. Synthesis of a peptide emulsifier with an amphiphilic structure. Biosci. Biotechnol. Biochem., 59: 388-392, 1995.
25. S. Turgeon, S.F. Gauthier, D. Molleé, J. Léonil. Interfacial properties of tryptic peptides of β-lactoglobulin. J. Agric. Food Chem., 40: 669-675, 1992.
26. A. Rau, R. Hogg, R. Marquardt, R. Hulgenfeld. A new lysozyme fold: crystal structure of the muramidase from Streptomyces coelicolor at 1.65? J. Biol. Chem., 276: 31994-31999, 2001.
27. J. Dou, S. Toma, S. Nakai. Random-centroid optimization for food formulation. Food Res. Int., 26: 27-37, 1993.
28. A. Madadi. Anti-invasive activity of bovine colostrums and whey proteins against Salmonella typhymurium. [Ph.D. thesis] Vancouver: University of British Columbia, 2003.
29. Z. Weng, C. DeLisi. Protein therapeutics; promises and challenges for the 21st century. Trends Biotechnol., 20: 29-35, 2002.
30. C. Sotriffer, G. Klee. Identification and mapping of small-molecule binding sites in proteins: Computational tools for structure-based design. Il Farmaco 57: 243-251, 2002.
31. Recombinant human lactoferrin. Immunotherapy Weekly, Nov.20, 2002 (www.newsrx.com/News/2002-11-20LW.html).
32. B.W.A. van der Strate, L. Beljaars, G. Molema, M.C. Harmsen, D.K.F. Meijer. Antiviral activities of lactoferrin. Antivir. Res., 52: 225-239, 2001.
33. D. Tomé, H. Debabbi. Physiological effects of milk protein components. Int. Dairy J., 8: 383-392, 1998.
34. P.P. Ward, S. Uribe-Luna, O.M. Conneely. Lactoferrin and host defense. Biochem. Cell Biol., 80: 95-102, 2002.
35. A.S. Naidu. Lactoferrin, In: A.S. Naidu (Ed.). Natural Food Antimicrobial Systems. Boca Raton, FL: CRC Press, 2000, 17-102.
36. P.F. Wang, D.L. Kaplan. Genetic engineering of fibrous proteins: spider dragline silk and collagen. Adv. Drug Deliv. Rev., 54: 1131-1143, 2002.
37. A. Wlodawer. Rational approach to AIDS drug design through structural biology. Annu. Rev. Med., 52: 595-614, 2002.