Homology Modeling and Docking Studies of Human Bcl-2L10 Protein |
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Authors: | T. Richard J. C. Delaunay J. M. Mérillon J. P. Monti |
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Affiliation: | 1. Laboratoire de physique et biophysique;2. Laboratoire de biotechnologie végétale GESVAB EA 3675 Faculté des Sciences Pharmaceutiques , Université de Bordeaux 2 , 146 rue Léo Saignat, 33076 , Bordeaux cedex , France |
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Abstract: | Abstract Bradykinin is a bioactive hormone involved in a variety of physiological processes. In various solvents, this peptide adopts β-turn structures. The C-terminal turn is a structural feature for the receptor affinity of agonists and antagonists while the N-terminal turn might be important for antagonistic activities. Polyphenols like dimeric proanthocyanidin B3 interact with the peptide. Thus to investigate the effects of polyphenols on bradykinin activity and structure, we studied the interaction in the structuring solvent DMSO which can be a close mimic of aqueous physiological environments like receptor-binding sites. Bradykinin alone presented a folded structure with two turns. B3 interacted with the peptide C-terminus and involved the loss of the bend structure of this region, while the N-ter-minus turn was maintained. Numerous studies have shown that polyphenolic molecules can act upon various biological targets, and the formation of this type of complex might be one of the possible modes of action. |
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Keywords: | Apoptosis Bcl-2 Bcl-2L10 BH3 domain Cancer therapy Comparative Modeling Molecular Docking |
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