Interaction between Bovine Serum Albumin with Lamivudine,Efavirenz,Tenofovir and Its Mechanism by Fluorescence Spectroscopy and Molecular Docking
10.6039/j.issn.1001-0408.2017.01.13
- VernacularTitle:荧光光谱法和分子对接研究拉米夫定、依非韦伦、替诺福韦与牛血清白蛋白的相互作用及机制
- Author:
Rong LIU
- Keywords:
Lamivudine;
Efavirenz;
Tenofovir;
Bovine serum albumin;
Fluorescence spectroscopy;
Molecular docking
- From:
China Pharmacy
2017;28(1):49-53
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVE:To study the interaction between bovine serum albumin(BSA)with lamivudine,efavirenz,tenofovir and its mechanism. METHODS:Fluorescence spectroscopy was used to determine the interaction between BSA with different con-centrations of lamivudine,efavirenz,tenofovir under different temperatures. The fluorescence intensity of them were determined re-spectively;quenching constant(KSV),apparent quenching constant(Kq),binding constant(KA),binding site(n),thermodynamic enthalpy change(ΔH),free energy diversification(ΔG)and entropy change(ΔS)were calculated according to Stern-Volmer equa-tion and so on. Molecular docking model of 3 drugs with BSA was established by using Sybyl 6.7 Flex X model. RESULTS:Kq for the interaction between 3 drugs with BSA were all higher than 2.0×1010 L/(mol·s),and were decreased with the increase of temper-ature;all n were close to 1,and thermodynamic functions ΔG<0,ΔS<0,ΔH<0. Molecular docking model showed that 3 drugs were mainly bound with BSA at Sudlow Ⅰ subdomain site. CONCLUSIONS:There are the interaction between 3 drugs with BSA;fluorescence quenching mainly manifests as static quenching;binding reaction belongs to spontaneous molecular action pro-cess;binding force mainly includes hydrogen bond and Van der Waals'force. The result of fluorescence experiment is consistent with those of molecular docking,and they complement each other.
