Gold Nanoparticle-Stabilized, Tyrosine-Rich Peptide Self-Assemblies and Their Catalytic Activities in the Reduction of 4-Nitrophenol

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초록

Peptides are suitable candidates for templates in the fabrication of various metal nanoparticles (NPs) because of their metal-binding ability and templating effect, which impart physicochemical properties to the produced nanoparticles. Peptide-binding gold nanoparticles (AuNPs) show high catalytic activity that permits their application in oxidation or reduction reactions. Herein, we prepared morphology-controllable AuNPs stabilized by self-assembled tyrosine rich peptides (YC7) by varying the pH and YC7 peptide/Au3+ concentration ratio in 2-(N-morpholino)ethanesulfonic acid (MES) buffer solution. The catalytic activities of the YC7 peptide-stabilized AuNPs (YC7@AuNPs) were tested for 4-nitrophenol (4-NP) reduction, and kinetic analysis was performed to calculate the apparent rate constants and activation energies. The relatively low activation energy of the YC7@AuNPs could be explained by the hypothesis that the tyrosine moiety of YC7 enriches the electron density of Au metal.

키워드

NANOSTRUCTURE; SIZE; MORPHOLOGY; SEQUENCE; BINDING; GROWTH
제목
Gold Nanoparticle-Stabilized, Tyrosine-Rich Peptide Self-Assemblies and Their Catalytic Activities in the Reduction of 4-Nitrophenol
저자
Lee, Namhun; Lee, Dae-Won; Lee, Sang-Myung
DOI
10.1021/acs.biomac.8b01221
발행일
2018-12
유형
Article
저널명
Biomacromolecules
권
19
호
12
페이지
4534 ~ 4541