Linked Life Data

18178096

Source:http://linkedlifedata.com/resource/pubmed/id/18178096

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-1-21
pubmed:abstractText
Human serum albumin (HSA) is a very important multi-domain transporter protein in the circulatory system responsible for carriage of various kinds of ligands within the physiological system. HSA is also known to undergo conformational transformation at different pH(s) and temperatures. In this report we have studied the binding interactions of a photosensitizing drug, protoporphyrin IX (PPIX) with various conformers of HSA at different temperatures using picosecond time-resolved fluorescence spectroscopy. Also, using dynamic light scattering (DLS) and circular dichroism (CD) spectroscopy we have followed the structural transition of various conformers of HSA at different temperatures. Ensuring the intact binding of PPIX to various conformers of HSA at different temperatures as revealed through time-resolved fluorescence anisotropy decay and significant spectral overlap of emission of Trp214 residue (donor) in domain-IIA and absorption of PPIX (acceptor) bound to domain-IB of HSA, we have applied Förster's resonance energy transfer (FRET) technique to determine the interdomain separation under various environmental conditions. The alkali-induced conformer of HSA shows almost no change in donor-acceptor distance in contrast to the native and acid-induced conformers of HSA, which show a decrease in distance with increase in temperature. Through this study the non-covalently bound PPIX is shown to be an efficient FRET probe in reporting the different temperature-induced folded states of HSA in buffer solutions of widely differing pH values.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1011-1344
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
90
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
69-77
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Spectroscopic studies on the effect of temperature on pH-induced folded states of human serum albumin.
pubmed:affiliation
Unit for Nano Science and Technology, Department of Chemical, Biological and Macromolecular Sciences, S.N. Bose National Centre for Basic Sciences, Block JD, Sector III, Salt Lake, Kolkata 700 098, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't