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Switchable Coacervate Formation via Amino Acid Functionalization of Poly(dehydroalanine).
Morrison, Casey A; Chan, Ethan P; Lee, Thatcher; Deming, Timothy J.
Afiliación
  • Morrison CA; Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California 90095, United States.
  • Chan EP; Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California 90095, United States.
  • Lee T; Department of Chemistry, Smith College, Northampton, Massachusetts 01063, United States.
  • Deming TJ; Department of Bioengineering, University of California, Los Angeles, Los Angeles, California 90095, United States.
Biomacromolecules ; 25(4): 2554-2562, 2024 Apr 08.
Article en En | MEDLINE | ID: mdl-38426942
ABSTRACT
Our group recently developed a family of side-chain amino acid-functionalized poly(S-alkyl-l-homocysteines), Xaa-CH (Xaa = generic amino acid), which possess the ability to form environmentally responsive coacervates in water. In an effort to further study how the molecular structure affects polypeptide coacervate formation, we prepared side-chain amino acid-functionalized poly(S-alkyl-rac-cysteines), Xaa-rac-C, via post-polymerization modification of poly(dehydroalanine), ADH. The use of the ADH platform allowed straightforward synthesis of a diverse range of side-chain amino acid-functionalized polypeptides via direct reaction of unprotected l-amino acid 2-mercaptoethylamides with ADH. Despite their differences in the main-chain structure, we found that Xaa-rac-C can form coacervates with properties similar to those seen with Xaa-CH. These results suggest that the incorporation of side-chain amino acids onto polypeptides may be a way to generally favor coacervation. The incorporation of l-methionine in Met-rac-C allowed the preparation of coacervates with improved stability against high ionic strength media. Further, the presence of additional thioether groups in Met-rac-C resulted in an increased solubility change upon oxidation allowing facile reversible redox switching of coacervate formation in aqueous media.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos / Alanina / Aminoácidos Idioma: En Revista: Biomacromolecules Asunto de la revista: BIOLOGIA MOLECULAR Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: 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 / Alanina / Aminoácidos Idioma: En Revista: Biomacromolecules Asunto de la revista: BIOLOGIA MOLECULAR Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos