Reversible "irreversible" inhibition of chymotrypsin using nanoparticle receptors.
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.
Molecular and Cellular Biology Program, University of Massachusetts, Amherst, Massachusetts 01003, USA.
Nicholas O
NO
Fischer
Ayush
A
Verma
Catherine M
CM
Goodman
Joseph M
JM
Simard
Vincent M
VM
Rotello
D002264:Carboxylic Acids / Q000737:chemistry*; D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D005454:Fluorescence Polarization; D006046:Gold / Q000737:chemistry*; D036103:Nanotechnology; D010316:Particle Size; D011489:Protein Denaturation; D055672:Static Electricity; D013499:Surface Properties; D013501:Surface-Active Agents / Q000737:chemistry
D002264:Carboxylic Acids; D013501:Surface-Active Agents; D006046:Gold; D002918:Chymotrypsin