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Stepwise Unfolding of Bovine and Human Serum Albumin by an Anionic Surfactant: An Investigation Using the Proton Transfer Probe Norharmane

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Title Stepwise Unfolding of Bovine and Human Serum Albumin by an
Anionic Surfactant: An Investigation Using the Proton Transfer Probe Norharmane
 
Creator Ghosh, Saptarshi
Chakrabarty, Satrajit
Bhowmik, Debipreeta
Kumar, Gopinatha Suresh
Chattopadhyay, Nitin
 
Subject Chemistry
 
Description Interactions of the anionic surfactant sodium dodecyl sulfate (SDS) with thetransport proteins bovine serum albumin (BSA) and human serum albumin (HSA) have
been divulged using an external photoinduced proton transfer probe, norharmane (NHM).Steady-state fluorometry, time-resolved measurements, micropolarity analysis, circular
dichroism (CD), and isothermal titration calorimetry (ITC) have been exploited for the study. With the gradual addition of SDS to the probe-bound proteins, the fluorometric responses of the different prototropic species of NHM exhibit an opposite pattern as to that observed while NHM binds to the proteins. The study reveals a sequential unfolding of the serum proteins with the gradual addition of SDS. ITC measures the heat changes associated
with each step of the unfolding. ITC experiments, carried out at two different pH’s, elucidate the nature of interaction between SDS and the two serum proteins. At a very high concentration of SDS, the external probe (NHM) is found to be dislodged from the protein environments to bind to the SDS micellar medium.
 
Publisher American Chemical Society
 
Date 2015
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/2235/1/JOURNAL_OF_PHYSICAL_CHEMISTRY_B__Volume_119___Issue_6___Special_Issue_SI___Pages_2090%2D2102_2015[54].pdf
Ghosh, Saptarshi and Chakrabarty, Satrajit and Bhowmik, Debipreeta and Kumar, Gopinatha Suresh and Chattopadhyay, Nitin (2015) Stepwise Unfolding of Bovine and Human Serum Albumin by an Anionic Surfactant: An Investigation Using the Proton Transfer Probe Norharmane. The Journal of Physical Chemistry B, 119. pp. 2090-2102.
 
Relation http://dx.doi.org/10.1021/jp501150p
http://www.eprints.iicb.res.in/2235/