A Femtosecond Study of the Interaction of Human Serum Albumin with a Surfactant (SDS)

Abstract

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.

Effect of ionic liquid on the native and denatured state of a protein covalently attached to a probe: Solvation dynamics study

“…It is observed that the native HSA exhibits two ultraslow solvation time components of 30 ps and 800 ps. 26 On addition of 1.5 M RTIL or 6 M GdnHCl to the native protein, one ultrafast component of 1 ps along with the ultraslow components (30 ps, 800ps for 1.5 M RTIL and 100 ps for 6 M GdnHCl) are observed. The average solvation time in presence of 1.5 M RTIL ( τ ∼260 ps) and 6 M GdnHCl ( τ ∼60 ps) becomes ∼2.5 times and ∼11 times faster, respectively, compared to that in native HSA ( τ ∼650 ps).…”

“…They were detected from a picosecond setup described in our earlier works. 26,47 The typical FWHM of the system response using a liquid scatterer is about 90 ps. The picosecond fluorescence decays were deconvoluted using IBH DAS6 software.…”

“…23,47 The samples were excited at 405 nm in our femtosecond up-conversion setup (FOG 100, CDP) described in our earlier works. 26,47 A cross-correlation function obtained using the Raman scattering from ethanol displayed a full width at half maximum (FWHM) of 350 fs. The femtosecond fluorescence decays were fitted using a Gaussian shape for the exciting pulse.…”

“…[15][16][17][18][19][20][21][22][23][24] and there is a considerable recent interest to understand dynamics of water near a protein. [25][26][27][28][29][30][31][32][33][34][35][36][37][38][39][40][41][42][43] Recent experimental, [25][26][27][28][29][30][31][32][39][40][41] theoretical, 34 and simulations [33][34][35][36][37][38] suggest that ''Biological Water'' near a protein could be 10 to 100 times slower than bulk water.…”

Antihypertensive activity of a quinoline appended chalcone derivative and its site specific binding interaction with a relevant target carrier protein

“…6,7 Amongst the foremost threat to cardiovascular and renal disorders, hypertension is a widespread and frequently progressive ailment. [12][13][14] BSA and Human Serum Albumin (HSA) are the most studied serum proteins in pharmaceutical industry due to their ability to bind various drug molecules and alter their pharmacokinetic/ pharmacodynamic properties. Among the many classes of antihypertensives, angiotensin converting enzyme (ACE) inhibitors are commonly used to treat cardiovascular diseases such as high blood pressure, heart failure, coronary/artery disease and kidney failure which inhibits the conversion of angiotensin I to angiotensin II.…”