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- W3141524562 abstract "von Willebrand factor (VWF) serves as a molecular bridge between the constituents of the suben- dothelium, such as collagen, and receptors of the platelet membrane, primarily GPIb. We have previously reported two monoclonal antibodies (mAbs), SZ-123 and SZ-125, which specifically bind the VWF A3 domain and block the interaction of VWF with collagen type III and ristocetin- or botrocetin-induced platelet aggregation. Here, we identi- fied the epitopes recognized by SZ-123 and SZ-125 using matrix-assisted laser desorption ionization mass spec- trometry in combination with proteolysis protection assays. Our results demonstrated that SZ-123 recognizes a dis- continuous epitope, involving the residues 989 AHLL SLVDVMQR 1000 and 1017 YLTSEMHGARPGASK 1031 of VWF. SZ-125 recognizes a linear epitope, encompassing the sequence 1001 EGGPSQIGDALGFAVR 1016 . Immuno- assays further indicated that the synthetic peptide, NH2- EGGPSQIGDALGFAVR-COOH, is sufficient for the binding to SZ-125. These results provide insight into the mechanistic basis for the inhibition of VWF binding to collagen by SZ-123/SZ-125." @default.
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- W3141524562 date "2011-01-01" @default.
- W3141524562 modified "2023-09-27" @default.
- W3141524562 title "Epitope mapping of human VWF A3 recognized by monoclonal antibody SZ-123 and SZ-125 using MALDI mass spectrometry" @default.
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