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A Femtosecond Study of the Interaction of Human Serum Albumin with a Surfactant (SDS)
Author(s) -
Mandal Ujjwal,
Ghosh Subhadip,
Mitra Gopa,
Adhikari Aniruddha,
Dey Shantanu,
Bhattacharyya Kankan
Publication year - 2008
Publication title -
chemistry – an asian journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.18
H-Index - 106
eISSN - 1861-471X
pISSN - 1861-4728
DOI - 10.1002/asia.200800114
Subject(s) - human serum albumin , sodium dodecyl sulfate , chemistry , solvation , pulmonary surfactant , molecule , femtosecond , chromatography , serum albumin , solvent , albumin , organic chemistry , biochemistry , laser , physics , optics
The interaction of a protein, human serum albumin (HSA) with a surfactant (sodium dodecyl sulfate, SDS) was studied by femtosecond up‐conversion. HSA was labeled covalently with a probe (CPM, 7‐dimethylamino‐3‐(4‐maleimidophenyl)‐4‐methylcoumarin). Binding of SDS to HSA is found to accelerate the solvation dynamics ∼1.3‐fold. The solvation dynamics in HSA displays two time components: 30 ps (20 %) and 800 ps (80 %). When ∼10 SDS molecules bind to HSA the components are 15 ps (40 %) and 800 ps (60 %). It is argued that SDS may increase the solvent exposure of the probe (CPM); it may also displace the buried water molecules in the immediate vicinity of CPM.