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Calcium-binding properties, stability, and osteogenic ability of phosphorylated soy peptide-calcium chelate
Bioactive peptides based on foodstuffs are of particular interest as carriers for calcium delivery due to their safety and high activity. The phosphorylated peptide has been shown to enhance calcium absorption and bone formation. A novel complex of peptide phosphorylation modification derived from s...
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Published in: | Frontiers in nutrition (Lausanne) 2023-04, Vol.10, p.1129548-1129548 |
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container_title | Frontiers in nutrition (Lausanne) |
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creator | Kong, Xiao Xiao, Ziqun Chen, Yuhang Du, MengDi Zhang, Zihui Wang, Zhenhua Xu, Bo Cheng, Yongqiang Yu, Tianying Gan, Jing |
description | Bioactive peptides based on foodstuffs are of particular interest as carriers for calcium delivery due to their safety and high activity. The phosphorylated peptide has been shown to enhance calcium absorption and bone formation.
A novel complex of peptide phosphorylation modification derived from soybean protein was introduced, and the mechanism, stability, and osteogenic differentiation bioactivity of the peptide with or without calcium were studied.
The calcium-binding capacity of phosphorylated soy peptide (SPP) reached 50.24 ± 0.20 mg/g. The result of computer stimulation and vibration spectrum showed that SPP could chelate with calcium by the phosphoric acid group, carboxyl oxygen of C-terminal Glu, Asp, and Arg, and phosphoric acid group of Ser on the SPP at a stoichiometric ratio of 1:1, resulting in the formation of the complex of ligand and peptide. Thermal stability showed that chelation enhanced peptide stability compared with SPP alone. Additionally,
results showed that SPP-Ca could facilitate osteogenic proliferation and differentiation ability.
SPP may function as a promising alternative to current therapeutic agents for bone loss. |
doi_str_mv | 10.3389/fnut.2023.1129548 |
format | article |
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A novel complex of peptide phosphorylation modification derived from soybean protein was introduced, and the mechanism, stability, and osteogenic differentiation bioactivity of the peptide with or without calcium were studied.
The calcium-binding capacity of phosphorylated soy peptide (SPP) reached 50.24 ± 0.20 mg/g. The result of computer stimulation and vibration spectrum showed that SPP could chelate with calcium by the phosphoric acid group, carboxyl oxygen of C-terminal Glu, Asp, and Arg, and phosphoric acid group of Ser on the SPP at a stoichiometric ratio of 1:1, resulting in the formation of the complex of ligand and peptide. Thermal stability showed that chelation enhanced peptide stability compared with SPP alone. Additionally,
results showed that SPP-Ca could facilitate osteogenic proliferation and differentiation ability.
SPP may function as a promising alternative to current therapeutic agents for bone loss.</description><identifier>ISSN: 2296-861X</identifier><identifier>EISSN: 2296-861X</identifier><identifier>DOI: 10.3389/fnut.2023.1129548</identifier><identifier>PMID: 37153921</identifier><language>eng</language><publisher>Switzerland: Frontiers Media S.A</publisher><subject>calcium supplement ; characterization ; Nutrition ; osteogenic differentiation ; peptide-calcium chelate ; phosphorylation ; thermal stability</subject><ispartof>Frontiers in nutrition (Lausanne), 2023-04, Vol.10, p.1129548-1129548</ispartof><rights>Copyright © 2023 Kong, Xiao, Chen, Du, Zhang, Wang, Xu, Cheng, Yu and Gan.</rights><rights>Copyright © 2023 Kong, Xiao, Chen, Du, Zhang, Wang, Xu, Cheng, Yu and Gan. 2023 Kong, Xiao, Chen, Du, Zhang, Wang, Xu, Cheng, Yu and Gan</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c466t-5f7a1db3fcf845734081e86c8060b172390d0221eb3930c1a3555aa960546fdb3</citedby><cites>FETCH-LOGICAL-c466t-5f7a1db3fcf845734081e86c8060b172390d0221eb3930c1a3555aa960546fdb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10160607/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10160607/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37153921$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kong, Xiao</creatorcontrib><creatorcontrib>Xiao, Ziqun</creatorcontrib><creatorcontrib>Chen, Yuhang</creatorcontrib><creatorcontrib>Du, MengDi</creatorcontrib><creatorcontrib>Zhang, Zihui</creatorcontrib><creatorcontrib>Wang, Zhenhua</creatorcontrib><creatorcontrib>Xu, Bo</creatorcontrib><creatorcontrib>Cheng, Yongqiang</creatorcontrib><creatorcontrib>Yu, Tianying</creatorcontrib><creatorcontrib>Gan, Jing</creatorcontrib><title>Calcium-binding properties, stability, and osteogenic ability of phosphorylated soy peptide-calcium chelate</title><title>Frontiers in nutrition (Lausanne)</title><addtitle>Front Nutr</addtitle><description>Bioactive peptides based on foodstuffs are of particular interest as carriers for calcium delivery due to their safety and high activity. The phosphorylated peptide has been shown to enhance calcium absorption and bone formation.
A novel complex of peptide phosphorylation modification derived from soybean protein was introduced, and the mechanism, stability, and osteogenic differentiation bioactivity of the peptide with or without calcium were studied.
The calcium-binding capacity of phosphorylated soy peptide (SPP) reached 50.24 ± 0.20 mg/g. The result of computer stimulation and vibration spectrum showed that SPP could chelate with calcium by the phosphoric acid group, carboxyl oxygen of C-terminal Glu, Asp, and Arg, and phosphoric acid group of Ser on the SPP at a stoichiometric ratio of 1:1, resulting in the formation of the complex of ligand and peptide. Thermal stability showed that chelation enhanced peptide stability compared with SPP alone. Additionally,
results showed that SPP-Ca could facilitate osteogenic proliferation and differentiation ability.
SPP may function as a promising alternative to current therapeutic agents for bone loss.</description><subject>calcium supplement</subject><subject>characterization</subject><subject>Nutrition</subject><subject>osteogenic differentiation</subject><subject>peptide-calcium chelate</subject><subject>phosphorylation</subject><subject>thermal stability</subject><issn>2296-861X</issn><issn>2296-861X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>DOA</sourceid><recordid>eNpVkU9vEzEQxS0EolXoB-CCfOTQDf6_9gmhCNpKlbiAxM3y2rOJy2a92N5K-fZsSKjag2XrzbzfjPUQek_JmnNtPvXjXNeMML6mlBkp9Ct0yZhRjVb01-tn7wt0VcoDIYRyJgUVb9EFb6nkhtFL9HvjBh_nfdPFMcRxi6ecJsg1QrnGpbouDrEerrEbA06lQtrCGD0-6zj1eNqlspx8GFyFgEs64AmmGgM0_sTGfgfH4jv0pndDgavzvUI_v339sblt7r_f3G2-3DdeKFUb2beOho73vtdCtlwQTUErr4kiHW0ZNyQQxih03HDiqeNSSueMIlKofjGu0N2JG5J7sFOOe5cPNrlo_wkpb61bfugHsEYypkMnA1Gt0NyZThHohWLGgOCLskKfT6xp7vYQPIw1u-EF9GVljDu7TY-WEqqWhduF8PFMyOnPDKXafSwehsGNkOZimaZUqpYqtbTSU6vPqZQM_dMcSuwxdHsM3R5Dt-fQF8-H5ws-Of5HzP8CsPSqEQ</recordid><startdate>20230421</startdate><enddate>20230421</enddate><creator>Kong, Xiao</creator><creator>Xiao, Ziqun</creator><creator>Chen, Yuhang</creator><creator>Du, MengDi</creator><creator>Zhang, Zihui</creator><creator>Wang, Zhenhua</creator><creator>Xu, Bo</creator><creator>Cheng, Yongqiang</creator><creator>Yu, Tianying</creator><creator>Gan, Jing</creator><general>Frontiers Media S.A</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20230421</creationdate><title>Calcium-binding properties, stability, and osteogenic ability of phosphorylated soy peptide-calcium chelate</title><author>Kong, Xiao ; Xiao, Ziqun ; Chen, Yuhang ; Du, MengDi ; Zhang, Zihui ; Wang, Zhenhua ; Xu, Bo ; Cheng, Yongqiang ; Yu, Tianying ; Gan, Jing</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c466t-5f7a1db3fcf845734081e86c8060b172390d0221eb3930c1a3555aa960546fdb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>calcium supplement</topic><topic>characterization</topic><topic>Nutrition</topic><topic>osteogenic differentiation</topic><topic>peptide-calcium chelate</topic><topic>phosphorylation</topic><topic>thermal stability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kong, Xiao</creatorcontrib><creatorcontrib>Xiao, Ziqun</creatorcontrib><creatorcontrib>Chen, Yuhang</creatorcontrib><creatorcontrib>Du, MengDi</creatorcontrib><creatorcontrib>Zhang, Zihui</creatorcontrib><creatorcontrib>Wang, Zhenhua</creatorcontrib><creatorcontrib>Xu, Bo</creatorcontrib><creatorcontrib>Cheng, Yongqiang</creatorcontrib><creatorcontrib>Yu, Tianying</creatorcontrib><creatorcontrib>Gan, Jing</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Frontiers in nutrition (Lausanne)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kong, Xiao</au><au>Xiao, Ziqun</au><au>Chen, Yuhang</au><au>Du, MengDi</au><au>Zhang, Zihui</au><au>Wang, Zhenhua</au><au>Xu, Bo</au><au>Cheng, Yongqiang</au><au>Yu, Tianying</au><au>Gan, Jing</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Calcium-binding properties, stability, and osteogenic ability of phosphorylated soy peptide-calcium chelate</atitle><jtitle>Frontiers in nutrition (Lausanne)</jtitle><addtitle>Front Nutr</addtitle><date>2023-04-21</date><risdate>2023</risdate><volume>10</volume><spage>1129548</spage><epage>1129548</epage><pages>1129548-1129548</pages><issn>2296-861X</issn><eissn>2296-861X</eissn><abstract>Bioactive peptides based on foodstuffs are of particular interest as carriers for calcium delivery due to their safety and high activity. The phosphorylated peptide has been shown to enhance calcium absorption and bone formation.
A novel complex of peptide phosphorylation modification derived from soybean protein was introduced, and the mechanism, stability, and osteogenic differentiation bioactivity of the peptide with or without calcium were studied.
The calcium-binding capacity of phosphorylated soy peptide (SPP) reached 50.24 ± 0.20 mg/g. The result of computer stimulation and vibration spectrum showed that SPP could chelate with calcium by the phosphoric acid group, carboxyl oxygen of C-terminal Glu, Asp, and Arg, and phosphoric acid group of Ser on the SPP at a stoichiometric ratio of 1:1, resulting in the formation of the complex of ligand and peptide. Thermal stability showed that chelation enhanced peptide stability compared with SPP alone. Additionally,
results showed that SPP-Ca could facilitate osteogenic proliferation and differentiation ability.
SPP may function as a promising alternative to current therapeutic agents for bone loss.</abstract><cop>Switzerland</cop><pub>Frontiers Media S.A</pub><pmid>37153921</pmid><doi>10.3389/fnut.2023.1129548</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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subjects | calcium supplement characterization Nutrition osteogenic differentiation peptide-calcium chelate phosphorylation thermal stability |
title | Calcium-binding properties, stability, and osteogenic ability of phosphorylated soy peptide-calcium chelate |
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