Probing protein-surfactant interaction by steady state and time-resolved fluorescence spectroscopy.
The microenvironment of the probe coumarin 153 (C-153) in 1% bovine serum albumin (BSA) is more hydrophobic in nature compared to that in pure micelles or protein-surfactant complexes. In the native state of protein, we have not observed any solvation using C-153 as a probe but we have observed a slow dynamics on protein surface using 8-anilino-1-naphthalenesulfonic acid (ANS) as a probe. This may be due to the location of the probe (C-153) in the hydrophobic, solvent-inaccessible pocket of the BSA. Solvation dynamics in the BSA-surfactant (SDS) complexes in the solution phase is markedly different from that in pure micelles. This is may be due to the formation of 'necklace and bead' structure in the complexes. The rotational motion is also severely hindered in the surface of the protein.
Hazra
Partha
P
Department of Chemistry, Indian Institute of Technology, WB 721302 Kharagpur, India.
Chakrabarty
Debdeep
D
Chakraborty
Anjan
A
Sarkar
Nilmoni
N
D000817:Anilino Naphthalenesulfonates / Q000737:chemistry; D000818:Animals; D002417:Cattle; D003374:Coumarins / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D005456:Fluorescent Dyes / Q000494:pharmacology; D008823:Micelles; D008956:Models, Chemical; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013501:Surface-Active Agents / Q000737:chemistry* / Q000378:metabolism; D013696:Temperature; D013997:Time Factors
D000817:Anilino Naphthalenesulfonates; D003374:Coumarins; D005456:Fluorescent Dyes; D008823:Micelles; D012709:Serum Albumin; D013501:Surface-Active Agents; C027132:1-anilino-8-naphthalenesulfonate; C030123:coumarin