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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Published in:Marine Drugs
Main Authors: Yunhai Yi, Yunyun Lv, Lijun Zhang, Jian Yang, Qiong Shi
Format: Article in Journal/Newspaper
Language:English
Published: MDPI AG 2018
Subjects:
Online Access:https://doi.org/10.3390/md16100365
https://doaj.org/article/a04b3372a9cb46a1bf8d134e4cd1f634
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spelling ftdoajarticles:oai:doaj.org/article:a04b3372a9cb46a1bf8d134e4cd1f634 2023-05-15T15:32:39+02:00 High Throughput Identification of Antihypertensive Peptides from Fish Proteome Datasets Yunhai Yi Yunyun Lv Lijun Zhang Jian Yang Qiong Shi 2018-10-01T00:00:00Z https://doi.org/10.3390/md16100365 https://doaj.org/article/a04b3372a9cb46a1bf8d134e4cd1f634 EN eng MDPI AG http://www.mdpi.com/1660-3397/16/10/365 https://doaj.org/toc/1660-3397 1660-3397 doi:10.3390/md16100365 https://doaj.org/article/a04b3372a9cb46a1bf8d134e4cd1f634 Marine Drugs, Vol 16, Iss 10, p 365 (2018) antihypertensive peptide fish protein hydrolysate high throughput identification hypertension collagen Biology (General) QH301-705.5 article 2018 ftdoajarticles https://doi.org/10.3390/md16100365 2022-12-30T23:32:28Z 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. Article in Journal/Newspaper Atlantic salmon Salmo salar Directory of Open Access Journals: DOAJ Articles Marine Drugs 16 10 365
institution Open Polar
collection Directory of Open Access Journals: DOAJ Articles
op_collection_id ftdoajarticles
language English
topic antihypertensive peptide
fish protein hydrolysate
high throughput identification
hypertension
collagen
Biology (General)
QH301-705.5
spellingShingle antihypertensive peptide
fish protein hydrolysate
high throughput identification
hypertension
collagen
Biology (General)
QH301-705.5
Yunhai Yi
Yunyun Lv
Lijun Zhang
Jian Yang
Qiong Shi
High Throughput Identification of Antihypertensive Peptides from Fish Proteome Datasets
topic_facet antihypertensive peptide
fish protein hydrolysate
high throughput identification
hypertension
collagen
Biology (General)
QH301-705.5
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.
format Article in Journal/Newspaper
author Yunhai Yi
Yunyun Lv
Lijun Zhang
Jian Yang
Qiong Shi
author_facet Yunhai Yi
Yunyun Lv
Lijun Zhang
Jian Yang
Qiong Shi
author_sort Yunhai Yi
title High Throughput Identification of Antihypertensive Peptides from Fish Proteome Datasets
title_short 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_sort high throughput identification of antihypertensive peptides from fish proteome datasets
publisher MDPI AG
publishDate 2018
url https://doi.org/10.3390/md16100365
https://doaj.org/article/a04b3372a9cb46a1bf8d134e4cd1f634
genre Atlantic salmon
Salmo salar
genre_facet Atlantic salmon
Salmo salar
op_source Marine Drugs, Vol 16, Iss 10, p 365 (2018)
op_relation http://www.mdpi.com/1660-3397/16/10/365
https://doaj.org/toc/1660-3397
1660-3397
doi:10.3390/md16100365
https://doaj.org/article/a04b3372a9cb46a1bf8d134e4cd1f634
op_doi https://doi.org/10.3390/md16100365
container_title Marine Drugs
container_volume 16
container_issue 10
container_start_page 365
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