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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ftmdpi:oai:mdpi.com:/1660-3397/16/10/365/ 2023-08-20T04:05:20+02:00 High Throughput Identification of Antihypertensive Peptides from Fish Proteome Datasets Yunhai Yi Yunyun Lv Lijun Zhang Jian Yang Qiong Shi agris 2018-10-02 application/pdf https://doi.org/10.3390/md16100365 EN eng Multidisciplinary Digital Publishing Institute https://dx.doi.org/10.3390/md16100365 https://creativecommons.org/licenses/by/4.0/ Marine Drugs; Volume 16; Issue 10; Pages: 365 antihypertensive peptide fish protein hydrolysate high throughput identification hypertension collagen Text 2018 ftmdpi https://doi.org/10.3390/md16100365 2023-07-31T21:45:35Z 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. Text Atlantic salmon Salmo salar MDPI Open Access Publishing Marine Drugs 16 10 365 |
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antihypertensive peptide fish protein hydrolysate high throughput identification hypertension collagen |
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antihypertensive peptide fish protein hydrolysate high throughput identification hypertension collagen 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 |
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 |
Text |
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 |
Multidisciplinary Digital Publishing Institute |
publishDate |
2018 |
url |
https://doi.org/10.3390/md16100365 |
op_coverage |
agris |
genre |
Atlantic salmon Salmo salar |
genre_facet |
Atlantic salmon Salmo salar |
op_source |
Marine Drugs; Volume 16; Issue 10; Pages: 365 |
op_relation |
https://dx.doi.org/10.3390/md16100365 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/md16100365 |
container_title |
Marine Drugs |
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16 |
container_issue |
10 |
container_start_page |
365 |
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1774715838060822528 |