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dc.contributor.authorShah, Dhawal
dc.contributor.authorLi, Jianguo
dc.contributor.authorShaikh, Abdul Rajjak
dc.contributor.authorRajagopalan, Raj
dc.date.accessioned2015-08-03T09:33:06Z
dc.date.available2015-08-03T09:33:06Z
dc.date.issued2011-09-21
dc.identifier.issn87567938
dc.identifier.pmid21948347
dc.identifier.doi10.1002/btpr.710
dc.identifier.urihttp://hdl.handle.net/10754/561877
dc.description.abstractWe 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).
dc.publisherWiley
dc.subjectArginine
dc.subjectPreferential interaction coefficient
dc.subjectProtein aggregation
dc.titleArginine-aromatic interactions and their effects on arginine-induced solubilization of aromatic solutes and suppression of protein aggregation
dc.typeArticle
dc.contributor.departmentKAUST Catalysis Center (KCC)
dc.identifier.journalBiotechnology Progress
dc.contributor.institutionChemical and Pharmaceutical Engineering Program, The Singapore-MIT Alliance, National University of Singapore, Singapore 117576, Singapore
dc.contributor.institutionDept. of Chemical and Biomolecular Engineering, National University of Singapore, Singapore 117576, Singapore
dc.contributor.institutionSingapore Eye Research Institute, Singapore
dc.contributor.institutionMiddle East Technical University, KKTC, Northern Cyprus Campus, Via Mersin 10, Güzelyurt, Turkey
kaust.personShaikh, Abdul Rajjak
dc.date.published-online2011-09-21
dc.date.published-print2012-01


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