000			a
999			_c11486 _d11486
003			OSt
005			20200923160040.0
008			200923b xxu||||| |||| 00| 0 eng d
040			_aAIKTC-KRRC _cAIKTC-KRRC
100			_912597 _aSaufi, Aimi Nabila Mohamad
245			_aFluorometric and Docking Analysis of the Complex Formation between an Anti-cancer Drug, Chlorambucil and Bovine Serum Albumin
250			_aVol.53(4), Oct-Dec
260			_aKarnataka _bAssociation of Pharmaceutical Teachers of India (APTI) _c2019
300			_a682-687p.
520			_aBackground: To characterize the interaction between chlorambucil (CHB) and the carrier protein, bovine serum albumin (BSA) in order to understand the transport of this drug in blood circulation. Methods: Fluorescence quenching titration method was used to examine the interaction of CHB with BSA by determining its binding constant and binding stoichiometry. The binding site identification was probed with molecular docking techniques. Results: Values of the Stern-Volmer constant (KSV), bimolecular quenching rate constant (kq)and binding constant (Ka)for CHB-BSA system were determined as 3.57×104 M−1, 5.67 × 1012 M−1 s−1 and5.58 × 104 M−1, respectively. Binding stoichiometry was found to be ~1.0, as obtained from the double logarithmic plot. The molecular docking results revealed that CHB binds to both Site I and Site II of BSA, however Site II was predicted to be the preferred binding site. Conclusion: The value of Ka suggested intermediate binding affinity between CHB and BSA with the binding stoichiometry of 1:1. CHB was found to have the binding preference at Site II of BSA due to formation of greater contacts
650		0	_94639 _aPHARMACEUTICS
700			_912598 _aNor Farrab, Wahidah Ridzwan
773	0		_x0019-5464 _tIndian journal of pharmaceutical education and research _dBengluru Association of Pharmaceutical Teachers of India (APTI)
856			_uhttps://www.ijper.org/sites/default/files/IndJPhaEdRes_53_4_682.pdf _yClick here
942			_2ddc _cAR