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Role of Macromolecular Crowding on Stability and Iron Release Kinetics of Serum Transferrin

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Role of Macromolecular Crowding on Stability and Iron Release Kinetics of Serum Transferrin
 
Creator Kumar, Shailesh
Sharma, Deepak
Kumar, Rajesh
 
Subject QR Microbiology
 
Description The macromolecular crowding influences the structural stability and functional properties of transferrin (Tf). The equilibrium as well as kinetic studies of Tf at different concentrations of crowding agents (dextran 40, dextran 70, and ficoll 70) and at a fixed concentration of dextran 40 under different concentrations of NaCl at pH 7.4 and 5.6 (±1) revealed that (i) the crowder environment increases the diferric-Tf (Fe2Tf) stability against iron loss and overall denaturation of the protein, (ii) both in the absence and presence of crowder, the presence of salt promotes the loss of iron and overall denaturation of Fe2Tf which is due to ionic screening of electrostatic interactions, (iii) the crowder environment retards iron release from monoferric N-lobe of Tf (FeNTf) by increasing enthalpic barrier, (iv) the retardation of iron release by crowding is enthalpically dominated than the entropic one, (v) both in the absence and presence of crowder, the presence of salt accelerates the iron release from FeNTf due to ionic screening of electrostatic interactions and anion binding to KISAB sites, and (vi) the crowders environment is unable to diminish (a) the salt-induced destabilization of Fe2Tf against the loss of iron and overall denaturation and (b) the anion effect and ionic screening of diffusive counterions responsible to promote iron release from FeNTf.
 
Publisher ACS
 
Date 2017
 
Type Article
PeerReviewed
 
Relation http://dx.doi.org/10.1021/acs.jpcb.7b05702
http://crdd.osdd.net/open/2070/
 
Identifier Kumar, Shailesh and Sharma, Deepak and Kumar, Rajesh (2017) Role of Macromolecular Crowding on Stability and Iron Release Kinetics of Serum Transferrin. The Journal of Physical Chemistry B, 121 (37). pp. 8669-8683. ISSN 1520-6106