Noncovalent modification of chymotrypsin surface using an amphiphilic polymer scaffold: implications in modulating protein function.
We report here on a new amphiphilic homopolymer that binds noncovalently to proteins. This polymer not only binds to the target protein chymotrypsin with submicromolar affinity but also stabilizes the native structure of the protein. Since the polymer-protein binding process is based on electrostatic interaction, the bound protein can be released from the polymer surface and reactivated either by increasing the ionic strength or by adding complementary cationic surfactants. The electrostatic binding of polymer to the protein results in a marked change in the substrate specificity of chymotrypsin.
Sandanaraj
Britto S
BS
Department of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, USA.
Vutukuri
Dharma Rao
DR
Simard
Joseph M
JM
Klaikherd
Akamol
A
Hong
Rui
R
Rotello
Vincent M
VM
Thayumanavan
S
S
D000818:Animals; D002417:Cattle; D002918:Chymotrypsin / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D002942:Circular Dichroism; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D008823:Micelles; D008968:Molecular Conformation; D010649:Phenylalanine / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism; D011108:Polymers / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D013050:Spectrometry, Fluorescence; D013379:Substrate Specificity; D013499:Surface Properties
D008823:Micelles; D011108:Polymers; D010649:Phenylalanine; C018389:N-succinylglycyl-phenylalanine-4-nitroanilide; D002918:Chymotrypsin