A femtosecond study of the interaction of human serum albumin with a surfactant (SDS).
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 approximately 1.3-fold. The solvation dynamics in HSA displays two time components: 30 ps (20 %) and 800 ps (80 %). When approximately 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.
Mandal
Ujjwal
U
Physical Chemistry Department, Indian Association for the Cultivation of Science, Jadavpur, Kolkata, India.
Ghosh
Subhadip
S
Mitra
Gopa
G
Adhikari
Aniruddha
A
Dey
Shantanu
S
Bhattacharyya
Kankan
K
D006801:Humans; D015394:Molecular Structure; D012709:Serum Albumin / Q000737:chemistry*; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013501:Surface-Active Agents / Q000737:chemistry*; D013816:Thermodynamics; D013997:Time Factors
D012709:Serum Albumin; D013501:Surface-Active Agents; D012967:Sodium Dodecyl Sulfate