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    Nucleation of α1-Antichymotrypsin polymerization

    Crowther, D.C. and Serpell, L.C. and Dafforn, T.R. and Gooptu, Bibek and Lomas, D.A. (2003) Nucleation of α1-Antichymotrypsin polymerization. Biochemistry 42 (8), pp. 2355-2363. ISSN 0006-2960.

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    Abstract

    Alpha1-antichymotrypsin is an acute phase plasma protein and a member of the serpin superfamily. We show here that wildtype α1-antichymotrypsin forms polymers between the reactive center loop of one molecule and the β-sheet A of a second at a rate that is dependent on protein concentration and the temperature of the reaction. The rate of polymerization was accelerated by seeding with polymers of α1-antichymotrypsin and a complex of α1-antichymotrypsin with an exogenous reactive loop peptide but not with reactive loop cleaved α1-antichymotrypsin or with polymers of other members of the serpin superfamily. Sonication of α1-antichymotrypsin polymers markedly increased the efficacy of seeding such that polymers were able to form under physiological conditions. Taken together, these data provide the first demonstration that serpin polymerization can result from seeding. This mechanism is analogous to the fibrillization of the Aβ1-42 peptide and may be important in the deposition of α1-antichymotrypsin in the plaques of Alzheimer's disease.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Research Centre: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Administrator
    Date Deposited: 24 Jun 2015 14:48
    Last Modified: 06 Dec 2016 10:42
    URI: http://eprints.bbk.ac.uk/id/eprint/12438

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