Large-scale mapping of bioactive peptides in structural and sequence space
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 th...
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| Autores principales: | , , |
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| Formato: | Articulo |
| Lenguaje: | Inglés |
| Publicado: |
2018
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| Materias: | |
| Acceso en línea: | http://sedici.unlp.edu.ar/handle/10915/98334 https://ri.conicet.gov.ar/11336/86386 http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0191063 |
| Aporte de: |
| Sumario: | 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. |
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