Interaction between Bovine Serum Albumin with Lamivudine,Efavirenz,Tenofovir and Its Mechanism by Fluorescence Spectroscopy and Molecular Docking / 中国药房
China Pharmacy
;
(12): 49-53, 2017.
Article
in Chinese
| WPRIM
| ID: wpr-507748
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Language:
Chinese
Journal:
China Pharmacy
Year:
2017
Type:
Article
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