Arginine-aromatic interactions and their effects on arginine-induced solubilization of aromatic solutes and suppression of protein aggregation

Handle URI:
http://hdl.handle.net/10754/561877
Title:
Arginine-aromatic interactions and their effects on arginine-induced solubilization of aromatic solutes and suppression of protein aggregation
Authors:
Shah, Dhawal; Li, Jianguo; Shaikh, Abdul Rajjak; Rajagopalan, Raj
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).
KAUST Department:
KAUST Catalysis Center (KCC)
Publisher:
Wiley-Blackwell
Journal:
Biotechnology Progress
Issue Date:
21-Sep-2011
DOI:
10.1002/btpr.710
PubMed ID:
21948347
Type:
Article
ISSN:
87567938
Appears in Collections:
Articles; KAUST Catalysis Center (KCC)

Full metadata record

DC FieldValue Language
dc.contributor.authorShah, Dhawalen
dc.contributor.authorLi, Jianguoen
dc.contributor.authorShaikh, Abdul Rajjaken
dc.contributor.authorRajagopalan, Rajen
dc.date.accessioned2015-08-03T09:33:06Zen
dc.date.available2015-08-03T09:33:06Zen
dc.date.issued2011-09-21en
dc.identifier.issn87567938en
dc.identifier.pmid21948347en
dc.identifier.doi10.1002/btpr.710en
dc.identifier.urihttp://hdl.handle.net/10754/561877en
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).en
dc.publisherWiley-Blackwellen
dc.subjectArginineen
dc.subjectPreferential interaction coefficienten
dc.subjectProtein aggregationen
dc.titleArginine-aromatic interactions and their effects on arginine-induced solubilization of aromatic solutes and suppression of protein aggregationen
dc.typeArticleen
dc.contributor.departmentKAUST Catalysis Center (KCC)en
dc.identifier.journalBiotechnology Progressen
dc.contributor.institutionChemical and Pharmaceutical Engineering Program, The Singapore-MIT Alliance, National University of Singapore, Singapore 117576, Singaporeen
dc.contributor.institutionDept. of Chemical and Biomolecular Engineering, National University of Singapore, Singapore 117576, Singaporeen
dc.contributor.institutionSingapore Eye Research Institute, Singaporeen
dc.contributor.institutionMiddle East Technical University, KKTC, Northern Cyprus Campus, Via Mersin 10, Güzelyurt, Turkeyen
kaust.authorShaikh, Abdul Rajjaken

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