Towards glycosylated networks of helical polypeptides


Wade Wang


Wade Wang, Aofei Liu, Paula T. Hammond

Author Affiliation: 

Department of Chemistry, Department of Chemical Engineering, Massachusetts Institute of Technology


Proteins are well known to fold into defined secondary structures, _-helices and _-sheets. The _-helical motif is commonly encountered in biological systems due to its ability to efficiently present amino acid side chains from a rigid rod-like core. Poly(_-propargyl-L-glutamate) (PPLG), a synthetic polypeptide formed from amino acids with alkyne side chains, recreates this natural structure in a synthetic system while incorporating the ability to conjugate different molecules or macromolecules at near 100% grafting efficiency through post polymerization modification by click chemistry. Thus, PPLG meets many of the requirements for biological applications such as low toxicity, biodegradability, and high tunability. In order to effectively adapt this synthetic polypeptide for biological applications, methodologies must be developed to effectively conjugate biologically relevant molecules to the side chains of PPLG. This poster describes various chemistries for the conjugation of carbohydrates to PPLG.