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Population-based heteropolymer design to mimic protein mixtures.
Ruan, Zhiyuan; Li, Shuni; Grigoropoulos, Alexandra; Amiri, Hossein; Hilburg, Shayna L; Chen, Haotian; Jayapurna, Ivan; Jiang, Tao; Gu, Zhaoyi; Alexander-Katz, Alfredo; Bustamante, Carlos; Huang, Haiyan; Xu, Ting.
Afiliação
  • Ruan Z; Department of Materials Science and Engineering, University of California Berkeley, Berkeley, CA, USA.
  • Li S; Department of Statistics, University of California Berkeley, Berkeley, CA, USA.
  • Grigoropoulos A; Department of Materials Science and Engineering, University of California Berkeley, Berkeley, CA, USA.
  • Amiri H; Institute for Quantitative Biosciences-QB3, University of California, Berkeley, CA, USA.
  • Hilburg SL; Department of Materials Science and Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA.
  • Chen H; Department of Materials Science and Engineering, University of California Berkeley, Berkeley, CA, USA.
  • Jayapurna I; Department of Materials Science and Engineering, University of California Berkeley, Berkeley, CA, USA.
  • Jiang T; Department of Materials Science and Engineering, University of California Berkeley, Berkeley, CA, USA.
  • Gu Z; Department of Chemistry, Xiamen University and The MOE Key Laboratory of Spectrochemical Analysis and Instrumentation, Xiamen, China.
  • Alexander-Katz A; Department of Materials Science and Engineering, University of California Berkeley, Berkeley, CA, USA.
  • Bustamante C; Departments of Chemistry and Biomedical Engineering, Northwestern University, Evanston, IL, USA.
  • Huang H; Department of Materials Science and Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA.
  • Xu T; Institute for Quantitative Biosciences-QB3, University of California, Berkeley, CA, USA.
Nature ; 615(7951): 251-258, 2023 03.
Article em En | MEDLINE | ID: mdl-36890370
ABSTRACT
Biological fluids, the most complex blends, have compositions that constantly vary and cannot be molecularly defined1. Despite these uncertainties, proteins fluctuate, fold, function and evolve as programmed2-4. We propose that in addition to the known monomeric sequence requirements, protein sequences encode multi-pair interactions at the segmental level to navigate random encounters5,6; synthetic heteropolymers capable of emulating such interactions can replicate how proteins behave in biological fluids individually and collectively. Here, we extracted the chemical characteristics and sequential arrangement along a protein chain at the segmental level from natural protein libraries and used the information to design heteropolymer ensembles as mixtures of disordered, partially folded and folded proteins. For each heteropolymer ensemble, the level of segmental similarity to that of natural proteins determines its ability to replicate many functions of biological fluids including assisting protein folding during translation, preserving the viability of fetal bovine serum without refrigeration, enhancing the thermal stability of proteins and behaving like synthetic cytosol under biologically relevant conditions. Molecular studies further translated protein sequence information at the segmental level into intermolecular interactions with a defined range, degree of diversity and temporal and spatial availability. This framework provides valuable guiding principles to synthetically realize protein properties, engineer bio/abiotic hybrid materials and, ultimately, realize matter-to-life transformations.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polímeros / Conformação Proteica / Proteínas / Dobramento de Proteína / Biomimética / Materiais Biomiméticos Idioma: En Ano de publicação: 2023 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polímeros / Conformação Proteica / Proteínas / Dobramento de Proteína / Biomimética / Materiais Biomiméticos Idioma: En Ano de publicação: 2023 Tipo de documento: Article