These results may reflect the fact that binding of a peptide to a

These results may reflect the fact that binding of a peptide to a protein (or enzyme) molecule may arise from non-specific interactions or else occur at a site that is associated with an activity other than the one of interest, and these scenarios

cannot be easily be ascertained by molecular simulations alone. Predictive models can be generated by QSAR analysis of physicochemical characteristics (size, charge, polarity, secondary structure, sequence) reported for specific activities of peptides. Zhou et al. [24●] used QSAR analysis in conjunction with quantum mechanics/molecular mechanics analysis of the structural basis and energetic profile involved in complexes of peptides with the ACE enzyme, to model ACE inhibitory activity and bitterness on peptide structural property and the interaction

profiles between ACE TAM Receptor inhibitor Veliparib research buy receptor and peptide ligands. The correlation between ACE-inhibition and bitterness was strongest for di-peptides, and decreased markedly for tri-peptides and tetra-peptides, which the authors explained as being due to the exponential increase in structural diversity with each additional amino acid in the peptide length. Moreover, structural and energetic analysis of ACE–peptide complexes indicated that while ACE-inhibitory potency suggested by binding energy increased from di-peptide to tri-peptide and tetra-peptide, insignificant changes were observed for longer peptides, presumably as the terminal BCKDHB residues reside out of the active pocket of the enzyme and thus have minor influence on the binding. Using a similar approach, Wang et al. [25] reported a positive significant relationship between ACE-inhibitory potency and antioxidative activity of tri-peptides, but only a modest correlation with bitterness, suggesting the potential to develop non-bitter functional peptide products with multiple bioactivities. As evident from the preceding discussion, a bioinformatics-driven approach can lead to the discovery of novel peptides. Holton et al. [16] remarked that the tremendous

strides in bioinformatics tools made in various disciplines including biotechnology, drug discovery, comparative genomics, molecular medicine and microbial genomics, have not been paralleled in food and nutrition science research, and the use of bioinformatics in food is ‘still in its infancy’. They proposed establishment of a Food-Wiki database (FoodWikiDB) for sharing and managing the vast content of data being continuously generated. However, even though bioinformatics can provide insight at the molecular level of specific peptide sequences that would be of interest for further investigation, its limitations must be acknowledged. For example, in silico approaches cannot easily predict the bioactivity of combinations of peptides that are present in protein hydrolysates or fractions. Furthermore, the reliability and utility of bioinformatics is heavily dependent on the data repository used for in silico analysis.

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