Effect of Ionic Strength on the Binding of α-Chymotrypsin to Nanoparticle Receptors

Negatively charged carboxylate-functionalized mixed monolayer protected clusters (MMPCs) effectively bind and inhibit α-chymotrypsin based on complementary electrostatic surface recognition. We demonstrate that this binding can be disrupted by varying the ionic strength of the medium. Enzyme activit...

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Bibliographic Details
Published in:Langmuir 2004-05, Vol.20 (10), p.4178-4181
Main Authors: Verma, Ayush, Simard, Joseph M, Rotello, Vincent M
Format: Article
Language:English
Subjects:
Animals
Carboxylic Acids
Cattle
Chymotrypsin - chemistry
Chymotrypsin - metabolism
Gold
Nanostructures - chemistry
Osmolar Concentration
Protein Binding
Protein Conformation
Static Electricity
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Summary:Negatively charged carboxylate-functionalized mixed monolayer protected clusters (MMPCs) effectively bind and inhibit α-chymotrypsin based on complementary electrostatic surface recognition. We demonstrate that this binding can be disrupted by varying the ionic strength of the medium. Enzyme activity in the presence of MMPCs increases from 5% to 97% of native activity as salt concentration is increased from 0 to 1.5 M. Variation of ionic strengths after complete binding over 13 h results only in a modest restoration of enzymatic activity (
ISSN:0743-7463
1520-5827
DOI:10.1021/la036183v