Antihypertensive Effects in Vitro and in Vivo of Novel Angiotensin-Converting Enzyme Inhibitory Peptides from Bovine Bone Gelatin Hydrolysate
In this study, we investigated the antihypertensive effects in vitro and in vivo of novel angiotensin-converting enzyme inhibitory (ACEI) peptides purified and identified from bovine bone gelatin hydrolysate (BGH). Thirteen ACEI peptides were identified from BGH, and among which, RGL-(Hyp)-GL and RG...
Gespeichert in:
| Veröffentlicht in: | Journal of agricultural and food chemistry 2020-01, Vol.68 (3), p.759-768 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 768 |
|---|---|
| container_issue | 3 |
| container_start_page | 759 |
| container_title | Journal of agricultural and food chemistry |
| container_volume | 68 |
| creator | Cao, Songmin Wang, Yi Hao, Yuejing Zhang, Wangang Zhou, Guanghong |
| description | In this study, we investigated the antihypertensive effects in vitro and in vivo of novel angiotensin-converting enzyme inhibitory (ACEI) peptides purified and identified from bovine bone gelatin hydrolysate (BGH). Thirteen ACEI peptides were identified from BGH, and among which, RGL-(Hyp)-GL and RGM-(Hyp)-GF exhibited high ACE inhibition with IC50 values of 1.44 and 10.23 μM. Molecular docking predicted that RGM-(Hyp)-GF and ACE residues of Glu384, His513, and Lys511 formed hydrogen-bonding interactions at distances of 2.57, 2.99, and 2.42 + 3.0 Å. RGL-(Hyp)-GL formed hydrogen bonds with Lys511 and Tyr523 and generated hydrogen-bonding interactions with His387 and Glu411 in the zinc(II) complexation motif at distances of 2.74 and 3.03 + 1.93 Å. The maximal decrements in systolic blood pressure in spontaneously hypertensive rats induced by one-time gavage of RGL-(Hyp)-GL and RGM-(Hyp)-GF at 30 mg/kg were 31.3 and 38.6 mmHg. RGL-(Hyp)-GL had higher enzyme degradation resistance than that of RGM-(Hyp)-GF in vitro incubation in rat plasma, and they were sequentially degraded into pentapeptides and tetrapeptides within 2 h. Our results indicate that BGH can serve as a nutritional candidate to control blood pressure. |
| doi_str_mv | 10.1021/acs.jafc.9b05618 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2327934330</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2327934330</sourcerecordid><originalsourceid>FETCH-LOGICAL-a402t-62635c1b6f05586502f556657230e8202f2a6f7a53a8cbe0fb8cf712bffe2e9c3</originalsourceid><addsrcrecordid>eNp1kUFvEzEQhS1ERUPhzgn5yKGbju141zmGKLSVqrYH4LryOuPW1a4dbGel5T_0P-M2gRuXGY3mfU-aeYR8YjBnwNmFNmn-pK2ZLzuQNVNvyIxJDpVkTL0lMyiaSpXFKXmf0hMAKNnAO3IqmFowwdWMPK98do_TDmNGn9yIdGMtmpyo8_SnyzFQ7beHYQw0WHobRuzpyj-48Ir4ah38WHjnH-jG_54GpNf-0XUuhzjRe9xlt8VEbQwD_RpG57G0Ui6x1wWiV9M2hn5KOuMHcmJ1n_DjsZ-RH98239dX1c3d5fV6dVPpBfBc1bwW0rCutiClqiVwK2Vdy4YLQMXLyHVtGy2FVqZDsJ0ytmG8K6dxXBpxRr4cfHcx_Npjyu3gksG-1x7DPrVc8GYpFkJAkcJBamJIKaJtd9ENOk4tg_YlhLaE0L6E0B5DKMjno_u-G3D7D_j79SI4Pwhe0bCPvhz7f78_g5KVTg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2327934330</pqid></control><display><type>article</type><title>Antihypertensive Effects in Vitro and in Vivo of Novel Angiotensin-Converting Enzyme Inhibitory Peptides from Bovine Bone Gelatin Hydrolysate</title><source>MEDLINE</source><source>ACS Publications</source><creator>Cao, Songmin ; Wang, Yi ; Hao, Yuejing ; Zhang, Wangang ; Zhou, Guanghong</creator><creatorcontrib>Cao, Songmin ; Wang, Yi ; Hao, Yuejing ; Zhang, Wangang ; Zhou, Guanghong</creatorcontrib><description>In this study, we investigated the antihypertensive effects in vitro and in vivo of novel angiotensin-converting enzyme inhibitory (ACEI) peptides purified and identified from bovine bone gelatin hydrolysate (BGH). Thirteen ACEI peptides were identified from BGH, and among which, RGL-(Hyp)-GL and RGM-(Hyp)-GF exhibited high ACE inhibition with IC50 values of 1.44 and 10.23 μM. Molecular docking predicted that RGM-(Hyp)-GF and ACE residues of Glu384, His513, and Lys511 formed hydrogen-bonding interactions at distances of 2.57, 2.99, and 2.42 + 3.0 Å. RGL-(Hyp)-GL formed hydrogen bonds with Lys511 and Tyr523 and generated hydrogen-bonding interactions with His387 and Glu411 in the zinc(II) complexation motif at distances of 2.74 and 3.03 + 1.93 Å. The maximal decrements in systolic blood pressure in spontaneously hypertensive rats induced by one-time gavage of RGL-(Hyp)-GL and RGM-(Hyp)-GF at 30 mg/kg were 31.3 and 38.6 mmHg. RGL-(Hyp)-GL had higher enzyme degradation resistance than that of RGM-(Hyp)-GF in vitro incubation in rat plasma, and they were sequentially degraded into pentapeptides and tetrapeptides within 2 h. Our results indicate that BGH can serve as a nutritional candidate to control blood pressure.</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/acs.jafc.9b05618</identifier><identifier>PMID: 31841328</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject><![CDATA[Angiotensin-Converting Enzyme Inhibitors - administration & dosage ; Angiotensin-Converting Enzyme Inhibitors - chemistry ; Angiotensin-Converting Enzyme Inhibitors - isolation & purification ; Animals ; Antihypertensive Agents - administration & dosage ; Antihypertensive Agents - chemistry ; Antihypertensive Agents - isolation & purification ; Blood Pressure - drug effects ; Bone and Bones - chemistry ; Cattle ; Gelatin - chemistry ; Humans ; Hypertension - drug therapy ; Hypertension - physiopathology ; Male ; Molecular Docking Simulation ; Peptides - administration & dosage ; Peptides - chemistry ; Peptides - isolation & purification ; Peptidyl-Dipeptidase A - chemistry ; Protein Hydrolysates - chemistry ; Rats ; Rats, Inbred SHR]]></subject><ispartof>Journal of agricultural and food chemistry, 2020-01, Vol.68 (3), p.759-768</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a402t-62635c1b6f05586502f556657230e8202f2a6f7a53a8cbe0fb8cf712bffe2e9c3</citedby><cites>FETCH-LOGICAL-a402t-62635c1b6f05586502f556657230e8202f2a6f7a53a8cbe0fb8cf712bffe2e9c3</cites><orcidid>0000-0001-6910-130X ; 0000-0002-8960-2141</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/acs.jafc.9b05618$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/acs.jafc.9b05618$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31841328$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cao, Songmin</creatorcontrib><creatorcontrib>Wang, Yi</creatorcontrib><creatorcontrib>Hao, Yuejing</creatorcontrib><creatorcontrib>Zhang, Wangang</creatorcontrib><creatorcontrib>Zhou, Guanghong</creatorcontrib><title>Antihypertensive Effects in Vitro and in Vivo of Novel Angiotensin-Converting Enzyme Inhibitory Peptides from Bovine Bone Gelatin Hydrolysate</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>In this study, we investigated the antihypertensive effects in vitro and in vivo of novel angiotensin-converting enzyme inhibitory (ACEI) peptides purified and identified from bovine bone gelatin hydrolysate (BGH). Thirteen ACEI peptides were identified from BGH, and among which, RGL-(Hyp)-GL and RGM-(Hyp)-GF exhibited high ACE inhibition with IC50 values of 1.44 and 10.23 μM. Molecular docking predicted that RGM-(Hyp)-GF and ACE residues of Glu384, His513, and Lys511 formed hydrogen-bonding interactions at distances of 2.57, 2.99, and 2.42 + 3.0 Å. RGL-(Hyp)-GL formed hydrogen bonds with Lys511 and Tyr523 and generated hydrogen-bonding interactions with His387 and Glu411 in the zinc(II) complexation motif at distances of 2.74 and 3.03 + 1.93 Å. The maximal decrements in systolic blood pressure in spontaneously hypertensive rats induced by one-time gavage of RGL-(Hyp)-GL and RGM-(Hyp)-GF at 30 mg/kg were 31.3 and 38.6 mmHg. RGL-(Hyp)-GL had higher enzyme degradation resistance than that of RGM-(Hyp)-GF in vitro incubation in rat plasma, and they were sequentially degraded into pentapeptides and tetrapeptides within 2 h. Our results indicate that BGH can serve as a nutritional candidate to control blood pressure.</description><subject>Angiotensin-Converting Enzyme Inhibitors - administration & dosage</subject><subject>Angiotensin-Converting Enzyme Inhibitors - chemistry</subject><subject>Angiotensin-Converting Enzyme Inhibitors - isolation & purification</subject><subject>Animals</subject><subject>Antihypertensive Agents - administration & dosage</subject><subject>Antihypertensive Agents - chemistry</subject><subject>Antihypertensive Agents - isolation & purification</subject><subject>Blood Pressure - drug effects</subject><subject>Bone and Bones - chemistry</subject><subject>Cattle</subject><subject>Gelatin - chemistry</subject><subject>Humans</subject><subject>Hypertension - drug therapy</subject><subject>Hypertension - physiopathology</subject><subject>Male</subject><subject>Molecular Docking Simulation</subject><subject>Peptides - administration & dosage</subject><subject>Peptides - chemistry</subject><subject>Peptides - isolation & purification</subject><subject>Peptidyl-Dipeptidase A - chemistry</subject><subject>Protein Hydrolysates - chemistry</subject><subject>Rats</subject><subject>Rats, Inbred SHR</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kUFvEzEQhS1ERUPhzgn5yKGbju141zmGKLSVqrYH4LryOuPW1a4dbGel5T_0P-M2gRuXGY3mfU-aeYR8YjBnwNmFNmn-pK2ZLzuQNVNvyIxJDpVkTL0lMyiaSpXFKXmf0hMAKNnAO3IqmFowwdWMPK98do_TDmNGn9yIdGMtmpyo8_SnyzFQ7beHYQw0WHobRuzpyj-48Ir4ah38WHjnH-jG_54GpNf-0XUuhzjRe9xlt8VEbQwD_RpG57G0Ui6x1wWiV9M2hn5KOuMHcmJ1n_DjsZ-RH98239dX1c3d5fV6dVPpBfBc1bwW0rCutiClqiVwK2Vdy4YLQMXLyHVtGy2FVqZDsJ0ytmG8K6dxXBpxRr4cfHcx_Npjyu3gksG-1x7DPrVc8GYpFkJAkcJBamJIKaJtd9ENOk4tg_YlhLaE0L6E0B5DKMjno_u-G3D7D_j79SI4Pwhe0bCPvhz7f78_g5KVTg</recordid><startdate>20200122</startdate><enddate>20200122</enddate><creator>Cao, Songmin</creator><creator>Wang, Yi</creator><creator>Hao, Yuejing</creator><creator>Zhang, Wangang</creator><creator>Zhou, Guanghong</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-6910-130X</orcidid><orcidid>https://orcid.org/0000-0002-8960-2141</orcidid></search><sort><creationdate>20200122</creationdate><title>Antihypertensive Effects in Vitro and in Vivo of Novel Angiotensin-Converting Enzyme Inhibitory Peptides from Bovine Bone Gelatin Hydrolysate</title><author>Cao, Songmin ; Wang, Yi ; Hao, Yuejing ; Zhang, Wangang ; Zhou, Guanghong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a402t-62635c1b6f05586502f556657230e8202f2a6f7a53a8cbe0fb8cf712bffe2e9c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Angiotensin-Converting Enzyme Inhibitors - administration & dosage</topic><topic>Angiotensin-Converting Enzyme Inhibitors - chemistry</topic><topic>Angiotensin-Converting Enzyme Inhibitors - isolation & purification</topic><topic>Animals</topic><topic>Antihypertensive Agents - administration & dosage</topic><topic>Antihypertensive Agents - chemistry</topic><topic>Antihypertensive Agents - isolation & purification</topic><topic>Blood Pressure - drug effects</topic><topic>Bone and Bones - chemistry</topic><topic>Cattle</topic><topic>Gelatin - chemistry</topic><topic>Humans</topic><topic>Hypertension - drug therapy</topic><topic>Hypertension - physiopathology</topic><topic>Male</topic><topic>Molecular Docking Simulation</topic><topic>Peptides - administration & dosage</topic><topic>Peptides - chemistry</topic><topic>Peptides - isolation & purification</topic><topic>Peptidyl-Dipeptidase A - chemistry</topic><topic>Protein Hydrolysates - chemistry</topic><topic>Rats</topic><topic>Rats, Inbred SHR</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cao, Songmin</creatorcontrib><creatorcontrib>Wang, Yi</creatorcontrib><creatorcontrib>Hao, Yuejing</creatorcontrib><creatorcontrib>Zhang, Wangang</creatorcontrib><creatorcontrib>Zhou, Guanghong</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cao, Songmin</au><au>Wang, Yi</au><au>Hao, Yuejing</au><au>Zhang, Wangang</au><au>Zhou, Guanghong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Antihypertensive Effects in Vitro and in Vivo of Novel Angiotensin-Converting Enzyme Inhibitory Peptides from Bovine Bone Gelatin Hydrolysate</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2020-01-22</date><risdate>2020</risdate><volume>68</volume><issue>3</issue><spage>759</spage><epage>768</epage><pages>759-768</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><abstract>In this study, we investigated the antihypertensive effects in vitro and in vivo of novel angiotensin-converting enzyme inhibitory (ACEI) peptides purified and identified from bovine bone gelatin hydrolysate (BGH). Thirteen ACEI peptides were identified from BGH, and among which, RGL-(Hyp)-GL and RGM-(Hyp)-GF exhibited high ACE inhibition with IC50 values of 1.44 and 10.23 μM. Molecular docking predicted that RGM-(Hyp)-GF and ACE residues of Glu384, His513, and Lys511 formed hydrogen-bonding interactions at distances of 2.57, 2.99, and 2.42 + 3.0 Å. RGL-(Hyp)-GL formed hydrogen bonds with Lys511 and Tyr523 and generated hydrogen-bonding interactions with His387 and Glu411 in the zinc(II) complexation motif at distances of 2.74 and 3.03 + 1.93 Å. The maximal decrements in systolic blood pressure in spontaneously hypertensive rats induced by one-time gavage of RGL-(Hyp)-GL and RGM-(Hyp)-GF at 30 mg/kg were 31.3 and 38.6 mmHg. RGL-(Hyp)-GL had higher enzyme degradation resistance than that of RGM-(Hyp)-GF in vitro incubation in rat plasma, and they were sequentially degraded into pentapeptides and tetrapeptides within 2 h. Our results indicate that BGH can serve as a nutritional candidate to control blood pressure.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>31841328</pmid><doi>10.1021/acs.jafc.9b05618</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0001-6910-130X</orcidid><orcidid>https://orcid.org/0000-0002-8960-2141</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-8561 |
| ispartof | Journal of agricultural and food chemistry, 2020-01, Vol.68 (3), p.759-768 |
| issn | 0021-8561 1520-5118 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2327934330 |
| source | MEDLINE; ACS Publications |
| subjects | Angiotensin-Converting Enzyme Inhibitors - administration & dosage Angiotensin-Converting Enzyme Inhibitors - chemistry Angiotensin-Converting Enzyme Inhibitors - isolation & purification Animals Antihypertensive Agents - administration & dosage Antihypertensive Agents - chemistry Antihypertensive Agents - isolation & purification Blood Pressure - drug effects Bone and Bones - chemistry Cattle Gelatin - chemistry Humans Hypertension - drug therapy Hypertension - physiopathology Male Molecular Docking Simulation Peptides - administration & dosage Peptides - chemistry Peptides - isolation & purification Peptidyl-Dipeptidase A - chemistry Protein Hydrolysates - chemistry Rats Rats, Inbred SHR |
| title | Antihypertensive Effects in Vitro and in Vivo of Novel Angiotensin-Converting Enzyme Inhibitory Peptides from Bovine Bone Gelatin Hydrolysate |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-05T07%3A18%3A21IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Antihypertensive%20Effects%20in%20Vitro%20and%20in%20Vivo%20of%20Novel%20Angiotensin-Converting%20Enzyme%20Inhibitory%20Peptides%20from%20Bovine%20Bone%20Gelatin%20Hydrolysate&rft.jtitle=Journal%20of%20agricultural%20and%20food%20chemistry&rft.au=Cao,%20Songmin&rft.date=2020-01-22&rft.volume=68&rft.issue=3&rft.spage=759&rft.epage=768&rft.pages=759-768&rft.issn=0021-8561&rft.eissn=1520-5118&rft_id=info:doi/10.1021/acs.jafc.9b05618&rft_dat=%3Cproquest_cross%3E2327934330%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2327934330&rft_id=info:pmid/31841328&rfr_iscdi=true |