Reversible "Irreversible" Inhibition of Chymotrypsin Using Nanoparticle Receptors

Nicholas O Fischer, Ayush Verma, Catherine M. Goodman, Joseph M. Simard, Vincent M. Rotello

Research output: Contribution to journalArticle

101 Scopus citations

Abstract

Anionically functionalized amphiphilic nanoparticles efficiently inhibit chymotrypsin through electrostatic binding followed by protein denaturation. We demonstrate the ability to disrupt this "irreversible" inhibition of chymotrypsin through modification of the nanoparticle surface using cationic surfactants. Up to 50% of original chymotrypsin activity is rescued upon long-chain surfactant addition. Dynamic light-scattering studies demonstrate that chymotrypsin is released from the nanoparticle surface. The conformation of the rescued chymotrypsin was characterized by fluorescence and fluorescence anisotropy, indicating that chymotrypsin regains a high degree of native structure upon surfactant addition.

Original languageEnglish (US)
Pages (from-to)13387-13391
Number of pages5
JournalJournal of the American Chemical Society
Volume125
Issue number44
DOIs
StatePublished - Nov 5 2003
Externally publishedYes

ASJC Scopus subject areas

  • Chemistry(all)

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