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Fabrication of a ferritin-casein phosphopeptide-calcium shell-core composite as a novel calcium delivery strategy
Plant ferritin has a natural cage-like nanospace for carrying bioactive ingredients. By taking advantage of the calcium binding ability of casein phosphopeptide (CPP) and the cage-like conformation of plant ferritin, a ferritin-CPP shell-core complex (FC) was fabricated with the reversible self-asse...
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Published in: | Food & function 2021-11, Vol.12 (22), p.11378-11386 |
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creator | Zhu, Lei Shi, Lina Wang, Qiao-E Meng, Demei Zhou, Zhongkai Yang, Rui |
description | Plant ferritin has a natural cage-like nanospace for carrying bioactive ingredients. By taking advantage of the calcium binding ability of casein phosphopeptide (CPP) and the cage-like conformation of plant ferritin, a ferritin-CPP shell-core complex (FC) was fabricated with the reversible self-assembly character of ferritin induced by a pH 2.0/7.0 transition strategy. The FC-calcium composite (FCC) was further fabricated by binding of the FC with calcium ions. When the same amount of calcium was loaded, the calcium binding capacity of the FCC was 28.13 ± 1.65%, which was significantly higher than that of ferritin and CPP alone. Fluorescence and Fourier transform infrared analysis indicated that the CPP encapsulation and the calcium binding in the FCC influenced the ferritin structure. Transmission electron microscopy (TEM) and dynamic light scattering (DLS) results showed that the spherical morphology and the 12 nm-diameter size were sustained in the FC and FCC. Moreover, the FCC as a transport carrier could increase the precipitation time of calcium phosphate, and the encapsulated calcium could be released in a more sustained manner as compared with ferritin and CPP under simulated
in vitro
gastrointestinal conditions. This study presents a novel calcium delivery strategy based on the ferritin cage and CPP, which will improve the applicability of ferritin and CPP and enhance the bioavailability of calcium ions.
Fabrication of a ferritin-casein phosphopeptide-calcium composite revealed a shell-core system with a sustained release of calcium ions. |
doi_str_mv | 10.1039/d1fo02134f |
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in vitro
gastrointestinal conditions. This study presents a novel calcium delivery strategy based on the ferritin cage and CPP, which will improve the applicability of ferritin and CPP and enhance the bioavailability of calcium ions.
Fabrication of a ferritin-casein phosphopeptide-calcium composite revealed a shell-core system with a sustained release of calcium ions.</description><identifier>ISSN: 2042-6496</identifier><identifier>EISSN: 2042-650X</identifier><identifier>DOI: 10.1039/d1fo02134f</identifier><identifier>PMID: 34671796</identifier><language>eng</language><publisher>England: Royal Society of Chemistry</publisher><subject>Binding ; Bioavailability ; Cages ; Calcium - chemistry ; Calcium ions ; Calcium phosphates ; Casein ; Caseins - chemistry ; Conformation ; Drug Carriers - chemistry ; Encapsulation ; Fabrication ; Ferritin ; Ferritins - chemistry ; Fluorescence ; Fourier analysis ; Fourier transforms ; Infrared analysis ; Ions ; Light scattering ; Morphology ; Nanocomposites - chemistry ; Phosphopeptides - chemistry ; Photon correlation spectroscopy ; Self-assembly ; Transmission electron microscopy</subject><ispartof>Food & function, 2021-11, Vol.12 (22), p.11378-11386</ispartof><rights>Copyright Royal Society of Chemistry 2021</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c337t-a7bcbebd684d6db8bfd90de4feb013fb1235ad07b62c3449d8be679d9533e3453</citedby><cites>FETCH-LOGICAL-c337t-a7bcbebd684d6db8bfd90de4feb013fb1235ad07b62c3449d8be679d9533e3453</cites><orcidid>0000-0002-7281-7672</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34671796$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhu, Lei</creatorcontrib><creatorcontrib>Shi, Lina</creatorcontrib><creatorcontrib>Wang, Qiao-E</creatorcontrib><creatorcontrib>Meng, Demei</creatorcontrib><creatorcontrib>Zhou, Zhongkai</creatorcontrib><creatorcontrib>Yang, Rui</creatorcontrib><title>Fabrication of a ferritin-casein phosphopeptide-calcium shell-core composite as a novel calcium delivery strategy</title><title>Food & function</title><addtitle>Food Funct</addtitle><description>Plant ferritin has a natural cage-like nanospace for carrying bioactive ingredients. By taking advantage of the calcium binding ability of casein phosphopeptide (CPP) and the cage-like conformation of plant ferritin, a ferritin-CPP shell-core complex (FC) was fabricated with the reversible self-assembly character of ferritin induced by a pH 2.0/7.0 transition strategy. The FC-calcium composite (FCC) was further fabricated by binding of the FC with calcium ions. When the same amount of calcium was loaded, the calcium binding capacity of the FCC was 28.13 ± 1.65%, which was significantly higher than that of ferritin and CPP alone. Fluorescence and Fourier transform infrared analysis indicated that the CPP encapsulation and the calcium binding in the FCC influenced the ferritin structure. Transmission electron microscopy (TEM) and dynamic light scattering (DLS) results showed that the spherical morphology and the 12 nm-diameter size were sustained in the FC and FCC. Moreover, the FCC as a transport carrier could increase the precipitation time of calcium phosphate, and the encapsulated calcium could be released in a more sustained manner as compared with ferritin and CPP under simulated
in vitro
gastrointestinal conditions. This study presents a novel calcium delivery strategy based on the ferritin cage and CPP, which will improve the applicability of ferritin and CPP and enhance the bioavailability of calcium ions.
Fabrication of a ferritin-casein phosphopeptide-calcium composite revealed a shell-core system with a sustained release of calcium ions.</description><subject>Binding</subject><subject>Bioavailability</subject><subject>Cages</subject><subject>Calcium - chemistry</subject><subject>Calcium ions</subject><subject>Calcium phosphates</subject><subject>Casein</subject><subject>Caseins - chemistry</subject><subject>Conformation</subject><subject>Drug Carriers - chemistry</subject><subject>Encapsulation</subject><subject>Fabrication</subject><subject>Ferritin</subject><subject>Ferritins - chemistry</subject><subject>Fluorescence</subject><subject>Fourier analysis</subject><subject>Fourier transforms</subject><subject>Infrared analysis</subject><subject>Ions</subject><subject>Light scattering</subject><subject>Morphology</subject><subject>Nanocomposites - chemistry</subject><subject>Phosphopeptides - chemistry</subject><subject>Photon correlation spectroscopy</subject><subject>Self-assembly</subject><subject>Transmission electron microscopy</subject><issn>2042-6496</issn><issn>2042-650X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNpd0U1r3DAQBmBRGroh3UvvLYJeQsCtZMmydSybbBII5NJCb0Yfo64W23IkO7D_Pkr2I1CB0CA9vAwahL5Q8oMSJn9a6gIpKePuAzovCS8LUZG_H481l2KBliltSV5MykY2n9CCcVHTWopz9LRWOnqjJh8GHBxW2EGMfvJDYVQCP-BxE1LeI4yTt5BvO-PnHqcNdF1hQgRsQj-G5CfAKuWAITxDh4_OQuefIe5wmqKa4N_uMzpzqkuwPJwX6M_65vfqrnh4vL1f_XooDGP1VKhaGw3aioZbYXWjnZXEAnegCWVO05JVypJai9IwzqVtNIhaWlkxBoxX7AJd7nPHGJ5mSFPb-2Ry02qAMKe2rJqKV1IIkun3_-g2zHHI3WUlG8IlKUVWV3tlYkgpgmvH6HsVdy0l7ess2mu6fnybxTrjb4fIWfdgT_T48xl83YOYzOn1fZjsBXobj9w</recordid><startdate>20211115</startdate><enddate>20211115</enddate><creator>Zhu, Lei</creator><creator>Shi, Lina</creator><creator>Wang, Qiao-E</creator><creator>Meng, Demei</creator><creator>Zhou, Zhongkai</creator><creator>Yang, Rui</creator><general>Royal Society of Chemistry</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>7T5</scope><scope>7T7</scope><scope>7TO</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-7281-7672</orcidid></search><sort><creationdate>20211115</creationdate><title>Fabrication of a ferritin-casein phosphopeptide-calcium shell-core composite as a novel calcium delivery strategy</title><author>Zhu, Lei ; Shi, Lina ; Wang, Qiao-E ; Meng, Demei ; Zhou, Zhongkai ; Yang, Rui</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c337t-a7bcbebd684d6db8bfd90de4feb013fb1235ad07b62c3449d8be679d9533e3453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Binding</topic><topic>Bioavailability</topic><topic>Cages</topic><topic>Calcium - chemistry</topic><topic>Calcium ions</topic><topic>Calcium phosphates</topic><topic>Casein</topic><topic>Caseins - chemistry</topic><topic>Conformation</topic><topic>Drug Carriers - chemistry</topic><topic>Encapsulation</topic><topic>Fabrication</topic><topic>Ferritin</topic><topic>Ferritins - chemistry</topic><topic>Fluorescence</topic><topic>Fourier analysis</topic><topic>Fourier transforms</topic><topic>Infrared analysis</topic><topic>Ions</topic><topic>Light scattering</topic><topic>Morphology</topic><topic>Nanocomposites - chemistry</topic><topic>Phosphopeptides - chemistry</topic><topic>Photon correlation spectroscopy</topic><topic>Self-assembly</topic><topic>Transmission electron microscopy</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhu, Lei</creatorcontrib><creatorcontrib>Shi, Lina</creatorcontrib><creatorcontrib>Wang, Qiao-E</creatorcontrib><creatorcontrib>Meng, Demei</creatorcontrib><creatorcontrib>Zhou, Zhongkai</creatorcontrib><creatorcontrib>Yang, Rui</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Food & function</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhu, Lei</au><au>Shi, Lina</au><au>Wang, Qiao-E</au><au>Meng, Demei</au><au>Zhou, Zhongkai</au><au>Yang, Rui</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fabrication of a ferritin-casein phosphopeptide-calcium shell-core composite as a novel calcium delivery strategy</atitle><jtitle>Food & function</jtitle><addtitle>Food Funct</addtitle><date>2021-11-15</date><risdate>2021</risdate><volume>12</volume><issue>22</issue><spage>11378</spage><epage>11386</epage><pages>11378-11386</pages><issn>2042-6496</issn><eissn>2042-650X</eissn><abstract>Plant ferritin has a natural cage-like nanospace for carrying bioactive ingredients. By taking advantage of the calcium binding ability of casein phosphopeptide (CPP) and the cage-like conformation of plant ferritin, a ferritin-CPP shell-core complex (FC) was fabricated with the reversible self-assembly character of ferritin induced by a pH 2.0/7.0 transition strategy. The FC-calcium composite (FCC) was further fabricated by binding of the FC with calcium ions. When the same amount of calcium was loaded, the calcium binding capacity of the FCC was 28.13 ± 1.65%, which was significantly higher than that of ferritin and CPP alone. Fluorescence and Fourier transform infrared analysis indicated that the CPP encapsulation and the calcium binding in the FCC influenced the ferritin structure. Transmission electron microscopy (TEM) and dynamic light scattering (DLS) results showed that the spherical morphology and the 12 nm-diameter size were sustained in the FC and FCC. Moreover, the FCC as a transport carrier could increase the precipitation time of calcium phosphate, and the encapsulated calcium could be released in a more sustained manner as compared with ferritin and CPP under simulated
in vitro
gastrointestinal conditions. This study presents a novel calcium delivery strategy based on the ferritin cage and CPP, which will improve the applicability of ferritin and CPP and enhance the bioavailability of calcium ions.
Fabrication of a ferritin-casein phosphopeptide-calcium composite revealed a shell-core system with a sustained release of calcium ions.</abstract><cop>England</cop><pub>Royal Society of Chemistry</pub><pmid>34671796</pmid><doi>10.1039/d1fo02134f</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-7281-7672</orcidid></addata></record> |
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subjects | Binding Bioavailability Cages Calcium - chemistry Calcium ions Calcium phosphates Casein Caseins - chemistry Conformation Drug Carriers - chemistry Encapsulation Fabrication Ferritin Ferritins - chemistry Fluorescence Fourier analysis Fourier transforms Infrared analysis Ions Light scattering Morphology Nanocomposites - chemistry Phosphopeptides - chemistry Photon correlation spectroscopy Self-assembly Transmission electron microscopy |
title | Fabrication of a ferritin-casein phosphopeptide-calcium shell-core composite as a novel calcium delivery strategy |
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