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  • Title: Inhibition of alternative pathway factor D by factor B-related synthetic hexapeptides.
    Author: Lesavre P, Gaillard MH, Halbwachs-Mecarelli L.
    Journal: Eur J Immunol; 1982 Mar; 12(3):252-4. PubMed ID: 6920299.
    Abstract:
    Hexapeptides mimicking the partial amino acid sequence of factor B surrounding the bond that is cleaved by factor D have been synthesized. These peptides have been assessed for their ability to inhibit factor D enzymatic activity and for their susceptibility to serine proteases. The synthetic peptides were cleaved by bovine trypsin and C1s but not by alpha-thrombin and factor D. The peptides inhibited factor B cleavage and fluid-phase or cell-bound alternative pathway C3 convertase activation by factor D. Altogether, these results suggest that peptides analogous to factor B specifically inhibit factor D enzymatic activity. Thus, they constitute an interesting tool for study of alternative pathway activation and can be of use when attempting to manipulate this pathway, since factor D is an essential component for alternative pathway initiation and amplification.
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