Effect of Arginine on Protein Aggregation Studied by Fluorescence Correlation Spectroscopy and Other Biophysical Methods
IR@IICB: CSIR-Indian Institute of Chemical Biology, KolkataView Archive Info
Effect of Arginine on Protein Aggregation Studied by Fluorescence Correlation
Spectroscopy and Other Biophysical Methods
Structural Biology & Bioinformatics
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.
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.