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

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    Type
    Article
    Authors
    Shah, Dhawal
    Li, Jianguo
    Shaikh, Abdul Rajjak
    Rajagopalan, Raj
    KAUST Department
    KAUST Catalysis Center (KCC)
    Date
    2011-09-21
    Online Publication Date
    2011-09-21
    Print Publication Date
    2012-01
    Permanent link to this record
    http://hdl.handle.net/10754/561877
    
    Metadata
    Show full item record
    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).
    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.710
    Publisher
    Wiley
    Journal
    Biotechnology Progress
    DOI
    10.1002/btpr.710
    PubMed ID
    21948347
    ae974a485f413a2113503eed53cd6c53
    10.1002/btpr.710
    Scopus Count
    Collections
    Articles; KAUST Catalysis Center (KCC)

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