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Effect of Arginine on Protein Aggregation Studied by Fluorescence Correlation Spectroscopy and Other Biophysical Methods

IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata

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Title Effect of Arginine on Protein Aggregation Studied by Fluorescence Correlation Spectroscopy and Other Biophysical Methods
 
Creator Ghosh, Ranendu
Sharma, Sunny
Chattopadhyay, Krishnananda
 
Subject Structural Biology & Bioinformatics
 
Description Arginine has been used extensively as an excipient in the formulation development of proteinbased biopharmaceuticals. We investigate the role of arginine in suppressing protein aggregation and its mechanism by using bovine serum albumin as a model system. By using sedimentation velocity and other analytical techniques, we show that the use of arginine inhibits temperature-induced aggregation of the protein. We use fluorescence correlation spectroscopy and other spectroscopic techniques to show that arginine inhibits accumulation of partially folded intermediates, potentially involved in the aggregation process. The hydrodynamic radii of the protein in its native, unfolded, and intermediate states have been determined using fluorescence correlation spectroscopy at single-molecule resolution. A possible mechanism of the effects of arginine and its role as an aggregation suppressor has been discussed.
 
Date 2009
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/136/1/BIOCHEMISTRY%2C48(_5)%2C1135%2D1143%2C2009[103].pdf
Ghosh, Ranendu and Sharma, Sunny and Chattopadhyay, Krishnananda (2009) Effect of Arginine on Protein Aggregation Studied by Fluorescence Correlation Spectroscopy and Other Biophysical Methods. Biochemistry, 48 (5). pp. 1135-1143.
 
Relation http://dx.doi.org/10.1021/bi802065j
http://www.eprints.iicb.res.in/136/