Biosynthetically derived glycopolypeptides for the manipulation of multivalent binding events

PMSE 112

Kristi L. Kiick, kiick@udel.edu, Department of Materials Science and Engineering, University of Delaware, 201 DuPont Hall, Newark, DE 19716
The biosynthesis of polypeptides and their subsequent chemical modification with saccharides offers a versatile strategy for the production of well-defined glycomacromolecules that provide insight into multivalent binding phenomena. Polypeptides equipped in select positions with novel chemically reactive amino acids have been produced via biosynthetic methods; the macromolecules adopt desired conformations that can be controlled with variations in temperature, pH, and salt concentration. The polypeptides can be modified with desired ligands via multiple chemical routes; the conformational behavior of the polypeptides is not compromised upon chemical modification. The binding of the glycopolypeptides to multiple lectin targets has been investigated via immunochemical and spectroscopic methods and indicates strategies for altering binding via specific differences in macromolecular structure. The versatility of the chemical routes available for the modification of engineered polypeptides suggests their potential in the manipulation of a variety of biologically relevant binding events.
 

Polypeptide and Protein Materials
8:00 AM-11:40 AM, Monday, August 20, 2007 Westin Boston Waterfront -- Commonwealth Blrm C, Oral

Division of Polymeric Materials: Science & Engineering

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007