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Anionic deep cavitands enable the adhesion of unmodified proteins at a membrane bilayer.
Ghang, Yoo-Jin; Perez, Lizeth; Morgan, Melissa A; Si, Fang; Hamdy, Omar M; Beecher, Consuelo N; Larive, Cynthia K; Julian, Ryan R; Zhong, Wenwan; Cheng, Quan; Hooley, Richard J.
Afiliación
  • Ghang YJ; University of California - Riverside, Department of Chemistry, Riverside, CA 92521, USA. richard.hooley@ucr.edu.
Soft Matter ; 10(48): 9651-6, 2014 Dec 28.
Article en En | MEDLINE | ID: mdl-25366572
ABSTRACT
An anionic self-folding deep cavitand is capable of immobilizing unmodified proteins and enzymes at a supported lipid bilayer interface, providing a simple, soft bioreactive surface that allows enzymatic function under mild conditions. The adhesion is based on complementary charge interactions, and the hosts are capable of binding enzymes such as trypsin at the bilayer interface the catalytic activity is retained upon adhesion, allowing selective reactions to be performed at the membrane surface.
Asunto(s)

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Resorcinoles / Proteínas / Éteres Cíclicos / Membrana Dobles de Lípidos Idioma: En Año: 2014 Tipo del documento: Article

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Resorcinoles / Proteínas / Éteres Cíclicos / Membrana Dobles de Lípidos Idioma: En Año: 2014 Tipo del documento: Article