scholarly journals Fluorometric and Docking Analysis of the Complex Formation between an Anti-Cancer Drug, Chlorambucil and Bovine Serum Albumin

2019 ◽  
Vol 53 (4) ◽  
pp. 682-687
Author(s):  
Aimi Nabila Mohamad Saufi ◽  
Nor Farrah Wahidah Ridzwan ◽  
Saharuddin Bin Mohamad ◽  
Saad Tayyab ◽  
Adyani Azizah Abd Halim

2012 ◽  
Vol 22 (13) ◽  
pp. 6053 ◽  
Author(s):  
Lili Xie ◽  
Weijun Tong ◽  
Dahai Yu ◽  
Jianquan Xu ◽  
Jun Li ◽  
...  


2015 ◽  
Vol 208 ◽  
pp. 304-313 ◽  
Author(s):  
J.A. Molina-Bolívar ◽  
F. Galisteo-González ◽  
C. Carnero Ruiz ◽  
M. Medina-O' Donnell ◽  
A. Parra




2021 ◽  
Vol 11 (5) ◽  
pp. 13102-13110

Novel (4R,12aS)-7-methoxy-4-methyl-6,8-dioxo-3,4,6,8,12,12a-hexahydro-2H-pyrido-[1',2':-4,5]-pyrazino[2,1-b][1,3]oxazine-9-carboxylic acid (L) was synthesized and characterised. The interaction between bovine serum albumin (BSA) with L was scrutinized by steady-state fluorescence spectroscopy, fluorescence anisotropy, fluorescence lifetime, and molecular docking methods. The fluorescence titration experiments of BSA resulted in fluorescence quenching with the incremental addition of L. The conformational binding of L to BSA has been investigated by molecular docking analysis. The molecular probe's best conformation showed the affinity as free binding energy release of -7.93 Kcal/mol. The docking analysis confirms that ligand binds in the near vicinity of TRP-213 in the binding pocket of subdomain IIA.



2018 ◽  
Vol 74 ◽  
pp. 267-274 ◽  
Author(s):  
Monique Barreto Santos ◽  
Carlos Wanderlei Piler de Carvalho ◽  
Edwin Elard Garcia-Rojas


2010 ◽  
Vol 11 (12) ◽  
pp. 3367-3374 ◽  
Author(s):  
T. Vinayahan ◽  
P. A. Williams ◽  
G. O. Phillips


Molecules ◽  
2019 ◽  
Vol 24 (17) ◽  
pp. 3056 ◽  
Author(s):  
Guiying Huang ◽  
Jun Liu ◽  
Weiping Jin ◽  
Zihao Wei ◽  
Chi-Tang Ho ◽  
...  

As a functional polysaccharide, inulin was carboxymethylated and it formed nanocomplexes with bovine serum albumin (BSA). The success of obtaining carboxymethyl inulin (CMI) was confirmed by a combination of Fourier transform Infrared (FT-IR), Raman spectroscopy, gel permeation chromatography (GPC), and titration. The effects of pH and ionic strength on the formation of CMI/BSA nanocomplexes were investigated. Our results showed that the formation of complex coacervate (pHφ1) and dissolution of CMI/BSA insoluble complexes (pHφ2) appeared in pH near 4.85 and 2.00 respectively. FT-IR and Raman data confirmed the existence of electrostatic interaction and hydrogen bonding between CMI and BSA. The isothermal titration calorimetry (ITC) results suggested that the process of complex formation was spontaneous and exothermic. The complexation was dominated by enthalpy changes (∆Η < 0, ∆S < 0) at pH 4.00, while it was contributed by enthalpic and entropic changes (∆Η < 0, ∆S > 0) at pH 2.60. Irregularly shaped insoluble complexes and globular soluble nanocomplexes (about 150 nm) were observed in CMI/BSA complexes at pH 4.00 and 2.60 while using optical microscopy and atomic force microscopy, respectively. The sodium chloride suppression effect on CMI/BSA complexes was confirmed by the decrease of incipient pH for soluble complex formation (or pHc) and pHφ1 under different sodium chloride concentrations. This research presents a new functional system with the potential for delivering bioactive food ingredients.





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