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High Throughput Identification of Antihypertensive Peptides from Fish Proteome Datasets

Antihypertensive peptides (AHTPs) are a group of small peptides with the main role to block key enzymes or receptors in the angiotensin genesis pathway. A great number of AHTPs have been isolated or digested from natural food resources; however, comprehensive studies on comparisons of AHTPs in vario...

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Autores principales: Yi, Yunhai, Lv, Yunyun, Zhang, Lijun, Yang, Jian, Shi, Qiong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6212880/
https://www.ncbi.nlm.nih.gov/pubmed/30279337
http://dx.doi.org/10.3390/md16100365
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author Yi, Yunhai
Lv, Yunyun
Zhang, Lijun
Yang, Jian
Shi, Qiong
author_facet Yi, Yunhai
Lv, Yunyun
Zhang, Lijun
Yang, Jian
Shi, Qiong
author_sort Yi, Yunhai
collection PubMed
description Antihypertensive peptides (AHTPs) are a group of small peptides with the main role to block key enzymes or receptors in the angiotensin genesis pathway. A great number of AHTPs have been isolated or digested from natural food resources; however, comprehensive studies on comparisons of AHTPs in various species from the perspective of big data are rare. Here, we established a simplified local AHTP database, and performed in situ mapping for high throughput identification of AHTPs with high antihypertensive activity from high-quality whole proteome datasets of 18 fish species. In the 35 identified AHTPs with reported high activity, we observed that Gly-Leu-Pro, Leu-Pro-Gly, and Val-Ser-Val are the major components of fish proteins, and AHTP hit numbers in various species demonstrated a similar distributing pattern. Interestingly, Atlantic salmon (Salmo salar) is in possession of far more abundant AHTPs compared with other fish species. In addition, collagen subunit protein is the largest group with more matching AHTPs. Further exploration of two collagen subunits (col4a5 and col8a1) in more fish species suggested that the hit pattern of these conserved proteins among teleost is almost the same, and their phylogeny is consistent with the evolution of these fish species. In summary, our present study provides basic information for the relationship of AHTPs with fish proteins, which sheds light on rapid discovery of marine drugs or food additives from fish protein hydrolysates to alleviate hypertension.
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spelling pubmed-62128802018-11-09 High Throughput Identification of Antihypertensive Peptides from Fish Proteome Datasets Yi, Yunhai Lv, Yunyun Zhang, Lijun Yang, Jian Shi, Qiong Mar Drugs Article Antihypertensive peptides (AHTPs) are a group of small peptides with the main role to block key enzymes or receptors in the angiotensin genesis pathway. A great number of AHTPs have been isolated or digested from natural food resources; however, comprehensive studies on comparisons of AHTPs in various species from the perspective of big data are rare. Here, we established a simplified local AHTP database, and performed in situ mapping for high throughput identification of AHTPs with high antihypertensive activity from high-quality whole proteome datasets of 18 fish species. In the 35 identified AHTPs with reported high activity, we observed that Gly-Leu-Pro, Leu-Pro-Gly, and Val-Ser-Val are the major components of fish proteins, and AHTP hit numbers in various species demonstrated a similar distributing pattern. Interestingly, Atlantic salmon (Salmo salar) is in possession of far more abundant AHTPs compared with other fish species. In addition, collagen subunit protein is the largest group with more matching AHTPs. Further exploration of two collagen subunits (col4a5 and col8a1) in more fish species suggested that the hit pattern of these conserved proteins among teleost is almost the same, and their phylogeny is consistent with the evolution of these fish species. In summary, our present study provides basic information for the relationship of AHTPs with fish proteins, which sheds light on rapid discovery of marine drugs or food additives from fish protein hydrolysates to alleviate hypertension. MDPI 2018-10-02 /pmc/articles/PMC6212880/ /pubmed/30279337 http://dx.doi.org/10.3390/md16100365 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Yi, Yunhai
Lv, Yunyun
Zhang, Lijun
Yang, Jian
Shi, Qiong
High Throughput Identification of Antihypertensive Peptides from Fish Proteome Datasets
title High Throughput Identification of Antihypertensive Peptides from Fish Proteome Datasets
title_full High Throughput Identification of Antihypertensive Peptides from Fish Proteome Datasets
title_fullStr High Throughput Identification of Antihypertensive Peptides from Fish Proteome Datasets
title_full_unstemmed High Throughput Identification of Antihypertensive Peptides from Fish Proteome Datasets
title_short High Throughput Identification of Antihypertensive Peptides from Fish Proteome Datasets
title_sort high throughput identification of antihypertensive peptides from fish proteome datasets
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6212880/
https://www.ncbi.nlm.nih.gov/pubmed/30279337
http://dx.doi.org/10.3390/md16100365
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