Reverse micelle induced flipping of binding site and efficiency of albumin protein with an ionic styryl dye.
The effect of reverse micelle environment on the binding mechanism of 2-(4-(dimethylamino)styryl)-1-methylpyridinium iodide (DASPMI) with Bovine Serum Albumin (BSA) compared with that in buffer solution has been investigated in this paper with the help of steady state and time-resolved emission spectroscopy along with molecular docking to have a correct picture about binding. The binding of DASPMI with attachment efficiency of 30% and 70% at site I (subdomain IIA) and site II (subdomain IIIA) of BSA, respectively, in buffer solution gets reversed inside a reverse micelle. The bigger cavity size of site II in buffer solution ushers the dye with increased attachment efficiency and in reverse micelle change in pi-stacking and hydrophobic interaction control the attachment efficiency. The calculated Forster distance gets curtailed as the environment changes from buffer to reverse micelle. The binding becomes stronger with a smaller gap between the probe and Trp-214 inside the reverse micelle than that in buffer solution.
Sahoo
Dibakar
D
Department of Spectroscopy, Indian Association for the Cultivation of Science, Jadavpur, Kolkata 700032, India.
Bhattacharya
Prosenjit
P
Chakravorti
Sankar
S
D000818:Animals; D016880:Anisotropy; D001665:Binding Sites; D002417:Cattle; D003198:Computer Simulation; D005456:Fluorescent Dyes / Q000737:chemistry*; D006801:Humans; D007477:Ions / Q000737:chemistry*; D008823:Micelles; D008958:Models, Molecular; D015394:Molecular Structure; D011487:Protein Conformation; D011726:Pyridinium Compounds / Q000737:chemistry*; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
D005456:Fluorescent Dyes; D007477:Ions; D008823:Micelles; D011726:Pyridinium Compounds; D012709:Serum Albumin; C011786:2-(4-(dimethylamino)styryl)-1-methylpyridinium