期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 125, 期 44, 页码 13387-13391出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja0352505
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资金
- NIGMS NIH HHS [GM 62998, GM08515] Funding Source: Medline
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.
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