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dc.contributor.authorGodwin, A.
dc.contributor.authorPedone, E.
dc.contributor.authorBalan, S.
dc.contributor.authorJumnah, R.
dc.contributor.authorBrocchini, S.
dc.contributor.authorChoi, J.-W.
dc.contributor.authorShaunak, S.
dc.contributor.authorZloh, Mire
dc.identifier.citationGodwin , A , Pedone , E , Balan , S , Jumnah , R , Brocchini , S , Choi , J-W , Shaunak , S & Zloh , M 2007 , ' Molecular dynamics simulations of proteins with chemically modified disulfide bonds ' , Theoretical Chemistry Accounts , vol. 117 , no. 2 , pp. 259-265 .
dc.identifier.otherPURE: 1448109
dc.identifier.otherPURE UUID: 1349da06-8137-47b3-b8b2-3000a736b6fb
dc.identifier.otherScopus: 33846629380
dc.descriptionCopyright 2007 Elsevier B.V., All rights reserved.
dc.description.abstractProteins 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.en
dc.relation.ispartofTheoretical Chemistry Accounts
dc.titleMolecular dynamics simulations of proteins with chemically modified disulfide bondsen
dc.contributor.institutionDepartment of Pharmacy
dc.contributor.institutionMedicinal and Analytical Chemistry
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.description.statusPeer reviewed
rioxxterms.typeJournal Article/Review

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