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Prototropism of [2,2 '-Bipyridyl]-3,3 '-diol in Albumin-SDS Aggregates

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Title Prototropism of [2,2 '-Bipyridyl]-3,3 '-diol in Albumin-SDS Aggregates
 
Creator DE, D
SANTRA, K
DATTA, A
 
Subject DOUBLE-PROTON-TRANSFER
PROTEIN-SURFACTANT INTERACTIONS
SODIUM DODECYL-SULFATE
HUMAN SERUM ALBUMINS
IONIC SURFACTANTS
BOVINE BSA
STATE
FLUORESCENCE
PROBE
SPECTROSCOPY
 
Description In this present investigation, attempt is made to use [2,2'-bipyridyl]-3,3'-diol (BP(OH)(2)) as a marker to study albumin-SDS interactions and to obtain structural information about these aggregates. It is also intended to contemplate the effect of these aggregates on the excited-state proton-transfer dynamics of BP(OH)(2). Steady-state and time-resolved fluorescence spectroscopic techniques are employed to elucidate the nature of interaction of two homologous carrier proteins, human serum albumin (HSA) and bovine serum albumin (BSA), with negatively charged surfactant sodium dodecyl sulfate (SDS). Both spectral and temporal behavior of BP(OH)(2) in these albumin SDS aggregates strongly affirm an initial competitive binding of SDS in high-energy binding sites of albumin. Unlike normal SDS micelles, the absence of formation of the monocation of BP(OH)(2) at the negatively charged interface of SDS is rationalized by screening of the micellar interface in the presence of denatured protein which wraps around these surfactant aggregates. An enhanced extent of excited-state proton transfer is manifested by a corresponding increase in fluorescence quantum yield of BP(OH)(2) in these aggregates. Temporal evolution of BP(OH)(2) at different emission wavelengths fortifies the formation of normal micelles post saturation. All our observations are found to corroborate with the necklace and bead model proposed for protein surfactant aggregates.
 
Publisher AMER CHEMICAL SOC
 
Date 2014-10-16T14:49:23Z
2014-10-16T14:49:23Z
2012
 
Type Article
 
Identifier JOURNAL OF PHYSICAL CHEMISTRY B, 116(37)11466-11472
http://dx.doi.org/10.1021/jp306027h
http://dspace.library.iitb.ac.in/jspui/handle/100/15826
 
Language en