Abstract
Health-enhancing potential bioactive peptide (BP) has driven an interest in food proteins as well as in the development of predictive methods. Research in this area has been especially active to use them as components in functional foods. Apparently, BPs do not have a given biological function in the containing proteins and they do not evolve under independent evolutionary constraints. In this work we performed a large-scale mapping of BPs in sequence and structural space. Using well curated BP deposited in BIOPEP database, we searched for exact matches in non-redundant sequences databases. Proteins containing BPs, were used in fold-recognition methods to predict the corresponding folds and BPs occurrences were mapped. We found that fold distribution of BP occurrences possibly reflects sequence relative abundance in databases. However, we also found that proteins with 5 or more than 5 BP in their sequences correspond to well populated protein folds, called superfolds. Also, we found that in well populated superfamilies, BPs tend to adopt similar locations in the protein fold, suggesting the existence of hotspots. We think that our results could contribute to the development of new bioinformatics pipeline to improve BP detection.
Highlights
As several endocrine and nervous systems in mammals are regulated by endogenous peptides, many of them could be regulated by exogenous peptides performing hormone-like functions [1]
To assess how structural information could be used in the identification of bioactive peptides, we performed a large-scale database sequence search followed by a structural mapping
Using BLAST searches against non-redundant database, we searched for proteins containing exact matches for each peptide more than 5 residues long taken from BIOPEP database [21]
Summary
As several endocrine and nervous systems in mammals are regulated by endogenous peptides, many of them could be regulated by exogenous peptides performing hormone-like functions [1]. Several works from food science and biotechnological areas have shown that several food proteins contain different amounts of these exogenous peptides [3,4]. These peptides are between 3 and 20 amino acids long and are found as encrypted regions in protein sequences.
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