<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-04-17T16:56:52Z</responseDate><request verb="GetRecord" identifier="oai:www.recercat.cat:2072/457895" metadataPrefix="marc">https://recercat.cat/oai/request</request><GetRecord><record><header><identifier>oai:recercat.cat:2072/457895</identifier><datestamp>2026-03-13T07:50:41Z</datestamp><setSpec>com_2072_98</setSpec><setSpec>col_2072_378192</setSpec></header><metadata><record xmlns="http://www.loc.gov/MARC21/slim" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://www.loc.gov/MARC21/slim http://www.loc.gov/standards/marcxml/schema/MARC21slim.xsd">
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      <subfield code="a">López-Laguna, Hèctor</subfield>
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      <subfield code="a">Sanchez, Julieta M.</subfield>
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      <subfield code="a">Carratalá, José Vicente</subfield>
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      <subfield code="a">Rojas Peña, Mauricio</subfield>
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      <subfield code="a">de Marco, Ario</subfield>
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      <subfield code="a">Roher Armentia, Nerea</subfield>
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      <subfield code="a">Unzueta Elorza, Ugutz</subfield>
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      <subfield code="a">Vázquez Gómez, Esther</subfield>
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      <subfield code="a">Villaverde Corrales, Antonio</subfield>
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      <subfield code="c">2021</subfield>
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      <subfield code="a">Altres ajuts: acords transformatius de la UAB</subfield>
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      <subfield code="a">We have developed a simple, robust, and fully transversal approach for thea-la-cartefabrication of functional multimeric nanoparticles with potential biomedical applications, validated here by a set of diverse and unrelated polypeptides. The proposed concept is based on the controlled coordination between Znions and His residues in His-tagged proteins. This approach results in a spontaneous and reproducible protein assembly as nanoscale oligomers that keep the original functionalities of the protein building blocks. The assembly of these materials is not linked to particular polypeptide features, and it is based on an environmentally friendly and sustainable approach. The resulting nanoparticles, with dimensions ranging between 10 and 15 nm, are regular in size, are architecturally stable, are fully functional, and serve as intermediates in a more complex assembly process, resulting in the formation of microscale protein materials. Since most of the recombinant proteins produced by biochemical and biotechnological industries and intended for biomedical research are His-tagged, the green biofabrication procedure proposed here can be straightforwardly applied to a huge spectrum of protein species for their conversion into their respective nanostructured formats.</subfield>
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      <subfield code="a">Nanoparticles</subfield>
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      <subfield code="a">Protein engineering</subfield>
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      <subfield code="a">Divalent cations</subfield>
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      <subfield code="a">Biomaterials design</subfield>
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      <subfield code="a">Biofabrication of functional protein nanoparticles through simple His-tag engineering</subfield>
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