作者: Vassilios Tsikaris , Marie-Christine Petit , Piotr Orlewski , Maria Sakarellos-Daitsiotis , Constantinos Sakarellos
DOI: 10.1007/BF02442896
关键词:
摘要: The I250 ASRYDQL257 synthetic octapeptide of theLeishmania major surface glycoprotein gp63, which efficiently inhibits parasite attachment to the macrophage receptors and mimics antigenically functionally RGDS sequence fibronectin, was studied by 2D TR-NOESY in presence an anti-SRYD monoclonal antibody (mAbSRYD) that recognizes both SRYD-containing peptides cognate protein on intact parasites. Molecular modeling performed using distance constraints obtained from TR-NOEs. bound structure compared with free peptide DMSO solution crystal RYD fragment OPG2 Fab, antireceptor RGD cell adhesion site.