Nanoengineered multivalent fertilinβ and cyritestin mimics for inhibition of fertilization

BIOL 227

Younjoo Lee, lee.younjoo@gmail.com and Nicole S. Sampson, nicole.sampson@stonybrook.edu. Department of Chemistry, Stony Brook University, Stony Brook, NY 11794
The sperm proteins fertilinβ and cyritestin, members of the ADAM family of proteins, are considered critical for mammalian sperm-egg binding. Previously, we reported a polymer designed to mimic fertilinβ by displaying the peptide ECD binds in a bivalent fashion with a spacer spanning 7-9 monomers. This polymer inhibited mouse in vitro fertilization 100-fold better than the corresponding monomeric peptide. In the present work, we prepared polymers of various lengths containing the peptide QCD to mimic cyritestin. These polymers range from 2 to 70 monomer units in length. QCD polymers 10 units in length or longer were better inhibitors than monomeric peptide, but their inhibition potency was 10 times worse than the corresponding ECD polymer inhibitors. A series of tri-block copolymers which have both ECD and QCD ligands displayed were tested to explore the relationship and degree of identity between fertilinβ and cyritestin receptors.
 

Frontiers in Chemical Biology
5:00 PM-7:00 PM, Wednesday, August 22, 2007 BCEC -- Exhibit Hall - B2, Poster

Division of Biological Chemistry

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