Design and synthesis of a chimeric TASP molecule as potential inhibitor in cell adhesion processes

The construction of protein-like folding motifs as structurally stable scaffolds for the introduction of function represents a major goal in protein design. The use of topol. templates allows the bypass of the well-known folding problem of linear polypeptides and offers a way to mimic native packing topologies by the template directed self-assembly of helical and/or b-sheeted peptide blocks. In conceptually sepg. structure from function, a chimeric 4-helix bundle TASP (Template Assembled Synthetic Protein) derived from the ROP protein and the cell adhesion glycoprotein E-selectin has been designed and synthesized, aimed at inhibiting an early stage in cell adhesion processes, in particular leukocyte adhesion. [on SciFinder (R)]

Published in:
Peptides for the New Millennium, Proceedings of the American Peptide Symposium, 16th , 519-520

 Record created 2006-02-09, last modified 2018-01-27

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