Arginine-aromatic interactions and their effects on arginine-induced solubilization of aromatic solutes and suppression of protein aggregation
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ArticleKAUST Department
KAUST Catalysis Center (KCC)Date
2011-09-21Online Publication Date
2011-09-21Print Publication Date
2012-01Permanent link to this record
http://hdl.handle.net/10754/561877
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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).Citation
Shah, D., Li, J., Shaikh, A. R., & Rajagopalan, R. (2011). Arginine-aromatic interactions and their effects on arginine-induced solubilization of aromatic solutes and suppression of protein aggregation. Biotechnology Progress, 28(1), 223–231. doi:10.1002/btpr.710Publisher
WileyJournal
Biotechnology ProgressDOI
10.1002/btpr.710PubMed ID
21948347ae974a485f413a2113503eed53cd6c53
10.1002/btpr.710
Scopus Count
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