Please use this identifier to cite or link to this item: https://doi.org/10.1002/btpr.710
Title: Arginine-aromatic interactions and their effects on arginine-induced solubilization of aromatic solutes and suppression of protein aggregation
Authors: Shah, D.
Li, J. 
Shaikh, A.R.
Rajagopalan, R. 
Keywords: Arginine
Preferential interaction coefficient
Protein aggregation
Issue Date: Jan-2012
Citation: Shah, D., Li, J., Shaikh, A.R., Rajagopalan, R. (2012-01). Arginine-aromatic interactions and their effects on arginine-induced solubilization of aromatic solutes and suppression of protein aggregation. Biotechnology Progress 28 (1) : 223-231. ScholarBank@NUS Repository. https://doi.org/10.1002/btpr.710
Abstract: We examine the interaction of aromatic residues of proteins with arginine, an additive commonly used to suppress protein aggregation, using experiments and molecular dynamics simulations. An aromatic-rich peptide, FFYTP (a segment of insulin), and lysozyme and insulin are used as model systems. Mass spectrometry shows that arginine increases the solubility of FFYTP by binding to the peptide, with the simulations revealing the predominant association of arginine to be with the aromatic residues. The calculations further show a positive preferential interaction coefficient, Γ XP, contrary to conventional thinking that positive Γ XP's indicate aggregation rather than suppression of aggregation. Simulations with lysozyme and insulin also show arginine's preference for aromatic residues, in addition to acidic residues. We use these observations and earlier results reported by us and others to discuss the possible implications of arginine's interactions with aromatic residues on the solubilization of aromatic moieties and proteins. Our results also highlight the fact that explanations based purely on Γ XP, which measures average affinity of an additive to a protein, could obscure or misinterpret the underlying molecular mechanisms behind additive-induced suppression of protein aggregation. © 2011 American Institute of Chemical Engineers (AIChE).
Source Title: Biotechnology Progress
URI: http://scholarbank.nus.edu.sg/handle/10635/88553
ISSN: 87567938
DOI: 10.1002/btpr.710
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

26
checked on Jul 17, 2018

WEB OF SCIENCETM
Citations

21
checked on Jun 27, 2018

Page view(s)

50
checked on Jun 1, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.