Direct Imaging of Protein Clusters in Metal–Organic Frameworks
Protein@metal–organic frameworks (P@MOFs) prepared by coprecipitation of protein, metal ions, and organic ligands represent an effective method for protein stabilization with a wide spectrum of applications. However, the formation mechanism of P@MOFs via the coprecipitation process and the reason wh...
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| Veröffentlicht in: | Journal of the American Chemical Society 2024-05, Vol.146 (18), p.12565-12576 |
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| container_end_page | 12576 |
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| container_title | Journal of the American Chemical Society |
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| creator | Liu, Yu Cui, Shitong Ma, Wenjun Wu, Yibo Xin, Ruobing Bai, Yunxiu Chen, Zhuo Xu, Jianhong Ge, Jun |
| description | Protein@metal–organic frameworks (P@MOFs) prepared by coprecipitation of protein, metal ions, and organic ligands represent an effective method for protein stabilization with a wide spectrum of applications. However, the formation mechanism of P@MOFs via the coprecipitation process and the reason why proteins can retain their biological activity in the frameworks with highly concentrated metal ions remain unsettled. Here, by a combined methodology of single molecule localization microscopy and clustering analysis, we discovered that in this process enzyme molecules form clusters with metal ions and organic ligands, contributing to both the nucleation and subsequent crystal growth. We proposed that the clusters played an important role in the retention of overall enzymatic activity by sacrificing protein molecules on the cluster surface. This work offers fresh perspectives on protein behaviors in the formation of P@MOFs, inspiring future endeavors in the design and development of artificial bionanocomposites with high biological activities. |
| doi_str_mv | 10.1021/jacs.4c01483 |
| format | Article |
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However, the formation mechanism of P@MOFs via the coprecipitation process and the reason why proteins can retain their biological activity in the frameworks with highly concentrated metal ions remain unsettled. Here, by a combined methodology of single molecule localization microscopy and clustering analysis, we discovered that in this process enzyme molecules form clusters with metal ions and organic ligands, contributing to both the nucleation and subsequent crystal growth. We proposed that the clusters played an important role in the retention of overall enzymatic activity by sacrificing protein molecules on the cluster surface. 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Am. Chem. Soc</addtitle><description>Protein@metal–organic frameworks (P@MOFs) prepared by coprecipitation of protein, metal ions, and organic ligands represent an effective method for protein stabilization with a wide spectrum of applications. However, the formation mechanism of P@MOFs via the coprecipitation process and the reason why proteins can retain their biological activity in the frameworks with highly concentrated metal ions remain unsettled. Here, by a combined methodology of single molecule localization microscopy and clustering analysis, we discovered that in this process enzyme molecules form clusters with metal ions and organic ligands, contributing to both the nucleation and subsequent crystal growth. We proposed that the clusters played an important role in the retention of overall enzymatic activity by sacrificing protein molecules on the cluster surface. This work offers fresh perspectives on protein behaviors in the formation of P@MOFs, inspiring future endeavors in the design and development of artificial bionanocomposites with high biological activities.</description><subject>bioactive properties</subject><subject>coprecipitation</subject><subject>enzyme activity</subject><subject>enzymes</subject><subject>ligands</subject><subject>Metal-Organic Frameworks - chemistry</subject><subject>microscopy</subject><subject>nanocomposites</subject><subject>Proteins - chemistry</subject><issn>0002-7863</issn><issn>1520-5126</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkD1PwzAQhi0EoqWwMaOMDKTc-SvuBioUkIrKAHPkOk6Vko9iJ0Js_Af-Ib8EVy2wICEP55Oee0_3EHKMMESgeL7Uxg-5AeSK7ZA-CgqxQCp3SR8AaJwoyXrkwPtlaDlVuE96TEmJQo765OKqcNa00V2lF0W9iJo8enBNa4s6Gpedb63zUfjf21aXn-8fM7fQdWGiidOVfW3csz8ke7kuvT3a1gF5mlw_jm_j6ezmbnw5jTVD3sYyExnL0SAwMGDmCSYJs6hEojiynGeKSivmnEoNIhllzAINRwmhpGGj8AbkdJO7cs1LZ32bVoU3tix1bZvOpwwFC_SIs_9R4FKgAC4CerZBjWu8dzZPV66otHtLEdK13nStN93qDfjJNrmbVzb7gb99_q5eTy2bztXByd9ZX-IqgTA</recordid><startdate>20240508</startdate><enddate>20240508</enddate><creator>Liu, Yu</creator><creator>Cui, Shitong</creator><creator>Ma, Wenjun</creator><creator>Wu, Yibo</creator><creator>Xin, Ruobing</creator><creator>Bai, Yunxiu</creator><creator>Chen, Zhuo</creator><creator>Xu, Jianhong</creator><creator>Ge, Jun</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><scope>7S9</scope><scope>L.6</scope><orcidid>https://orcid.org/0000-0001-5503-8899</orcidid><orcidid>https://orcid.org/0000-0002-3550-1345</orcidid></search><sort><creationdate>20240508</creationdate><title>Direct Imaging of Protein Clusters in Metal–Organic Frameworks</title><author>Liu, Yu ; Cui, Shitong ; Ma, Wenjun ; Wu, Yibo ; Xin, Ruobing ; Bai, Yunxiu ; Chen, Zhuo ; Xu, Jianhong ; Ge, Jun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a314t-6d5d3f1c1030c0cb71773e18578413f4d826e5b426a0579d3e024c05586c39393</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>bioactive properties</topic><topic>coprecipitation</topic><topic>enzyme activity</topic><topic>enzymes</topic><topic>ligands</topic><topic>Metal-Organic Frameworks - chemistry</topic><topic>microscopy</topic><topic>nanocomposites</topic><topic>Proteins - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liu, Yu</creatorcontrib><creatorcontrib>Cui, Shitong</creatorcontrib><creatorcontrib>Ma, Wenjun</creatorcontrib><creatorcontrib>Wu, Yibo</creatorcontrib><creatorcontrib>Xin, Ruobing</creatorcontrib><creatorcontrib>Bai, Yunxiu</creatorcontrib><creatorcontrib>Chen, Zhuo</creatorcontrib><creatorcontrib>Xu, Jianhong</creatorcontrib><creatorcontrib>Ge, Jun</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><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liu, Yu</au><au>Cui, Shitong</au><au>Ma, Wenjun</au><au>Wu, Yibo</au><au>Xin, Ruobing</au><au>Bai, Yunxiu</au><au>Chen, Zhuo</au><au>Xu, Jianhong</au><au>Ge, Jun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Direct Imaging of Protein Clusters in Metal–Organic Frameworks</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2024-05-08</date><risdate>2024</risdate><volume>146</volume><issue>18</issue><spage>12565</spage><epage>12576</epage><pages>12565-12576</pages><issn>0002-7863</issn><issn>1520-5126</issn><eissn>1520-5126</eissn><abstract>Protein@metal–organic frameworks (P@MOFs) prepared by coprecipitation of protein, metal ions, and organic ligands represent an effective method for protein stabilization with a wide spectrum of applications. However, the formation mechanism of P@MOFs via the coprecipitation process and the reason why proteins can retain their biological activity in the frameworks with highly concentrated metal ions remain unsettled. Here, by a combined methodology of single molecule localization microscopy and clustering analysis, we discovered that in this process enzyme molecules form clusters with metal ions and organic ligands, contributing to both the nucleation and subsequent crystal growth. We proposed that the clusters played an important role in the retention of overall enzymatic activity by sacrificing protein molecules on the cluster surface. This work offers fresh perspectives on protein behaviors in the formation of P@MOFs, inspiring future endeavors in the design and development of artificial bionanocomposites with high biological activities.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>38661569</pmid><doi>10.1021/jacs.4c01483</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0001-5503-8899</orcidid><orcidid>https://orcid.org/0000-0002-3550-1345</orcidid></addata></record> |
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| subjects | bioactive properties coprecipitation enzyme activity enzymes ligands Metal-Organic Frameworks - chemistry microscopy nanocomposites Proteins - chemistry |
| title | Direct Imaging of Protein Clusters in Metal–Organic Frameworks |
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