Modulation of the catalytic behavior of α-chymotrypsin at monolayer-protected nanoparticle surfaces

被引：0
|
作者：
You, Chang-Cheng [1 ]
Agasti, Sarit S. [1 ]
De, Mrinmoy [1 ]
Knapp, Michael J. [1 ]
Rotello, Vincent M. [1 ]
机构：
[1] Department of Chemistry, University of Massachusetts, 710 North Pleasant Street, Amherst, MA 01003, United States
来源：
Journal of the American Chemical Society | 2006年 / 128卷 / 45期
关键词：
Amino-acid-functionalized gold clusters modulate the catalytic behavior of α-chymotrypsin (ChT) toward cationic; neutral; and anionic substrates. Kinetic studies reveal that the substrate specificity (kcat/K M) of ChT-nanoparticle complexes increases by ∼3-fold for the cationic substrate but decreases by 95% for the anionic substrate as compared with that of free ChT; providing enhanced substrate selectivity. Concurrently; the catalytic constants (kcat) of ChT show slight augmentation for the cationic substrate and significant attenuation for the anionic substrate in the presence of amino-acid-functionalized nanoparticles. The amino acid monolayer on the nanoparticle is proposed to control both the capture of substrate by the active site and release of product through electrostatic interactions; leading to the observed substrate specificities and catalytic constants. © 2006 American Chemical Society;
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摘要：
Journal article (JA)
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页码：14612 / 14618
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