Your browser doesn't support javascript.
loading
Active Controlled and Tunable Coacervation Using Side-Chain Functional α-Helical Homopolypeptides.
Scott, Wendell A; Gharakhanian, Eric G; Bell, Alexandra G; Evans, Declan; Barun, Ehab; Houk, K N; Deming, Timothy J.
Afiliación
  • Scott WA; Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California 90095, United States.
  • Gharakhanian EG; Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California 90095, United States.
  • Bell AG; Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California 90095, United States.
  • Evans D; Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California 90095, United States.
  • Barun E; Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California 90095, United States.
  • Houk KN; Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California 90095, United States.
  • Deming TJ; Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California 90095, United States.
J Am Chem Soc ; 143(43): 18196-18203, 2021 11 03.
Article en En | MEDLINE | ID: mdl-34669392
ABSTRACT
We report the development of new side-chain amino acid-functionalized α-helical homopolypeptides that reversibly form coacervate phases in aqueous media. The designed multifunctional nature of the side-chains was found to provide a means to actively control coacervation via mild, biomimetic redox chemistry as well as allow response to physiologically relevant environmental changes in pH, temperature, and counterions. These homopolypeptides were found to possess properties that mimic many of those observed in natural coacervate forming intrinsically disordered proteins. Despite ordered α-helical conformations that are thought to disfavor coacervation, molecular dynamics simulations of a polypeptide model revealed a high degree of side-chain conformational disorder and hydration around the ordered backbone, which may explain the ability of these polypeptides to form coacervates. Overall, the modular design, uniform nature, and ordered chain conformations of these polypeptides were found to provide a well-defined platform for deconvolution of molecular elements that influence biopolymer coacervation and tuning of coacervate properties for downstream applications.
Asunto(s)
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos / Suspensiones / Aminoácidos Idioma: En Revista: J Am Chem Soc Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos / Suspensiones / Aminoácidos Idioma: En Revista: J Am Chem Soc Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos