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        Molecular dynamics simulations of proteins with chemically modified disulfide bonds

        Author
        Godwin, A.
        Pedone, E.
        Balan, S.
        Jumnah, R.
        Brocchini, S.
        Choi, J.-W.
        Shaunak, S.
        Zloh, Mire
        Attention
        2299/11601
        Abstract
        Proteins that are used as therapeutic drugs act in the extracellular microenvironment. They usually have a small number of intramolecular disulfide bonds to help maintain their tertiary structure in the vascular circulation. In general, most cysteine residues are part of a disulfide bond with free sulfhydrals being uncommon. We have studied whether the site-specific chemical reduction of disulfides and the incorporation of a 3-carbon methylene bridge between the cysteines in interferon-α 2a would change the structure of this protein. Bridging of both of the disulfide bonds of interferon-α 2a was studied using two different molecular simulation protocols: (1) molecular dynamics, and (2) stochastic dynamics. We have shown that the disulfide bonds in interferon-α 2a can be reduced and chemically modified without significantly altering the tertiary structure of the protein. This offers the novel possibility of chemically modifying therapeutically important proteins without affecting their biological properties.
        Publication date
        2007-02
        Published in
        Theoretical Chemistry Accounts
        Published version
        https://doi.org/10.1007/s00214-006-0134-0
        Other links
        http://hdl.handle.net/2299/11601
        Relations
        School of Life and Medical Sciences
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