SELECTION OF PHAGE DISPLAY COMBINATORIAL LIBRARY PEPTIDES WITH AFFINITY FOR A YOHIMBINE IMPRINTED METHACRYLATE POLYMER

alpha(2)-Adrenoreceptor mimics, prepared by molecular imprinting of yo himbine, were used to select ligands from a phage display hexapeptide library, Phages with affinity for the yohimbine imprinted methacrylic acid-ethylene glycol dimethacrylate copolymer were selected, Phage aff inities were estimated using an enzyme immunoassay, The selected libra ry showed three-fold higher affinity for the imprinted polymer compare d with the primary library, Eighty-two of ninety characterized phage c lones from the selected library showed low affinity for the polymer, T he hexapeptides on eight of these low binding phage clones consisted o f mainly hydrophobic amino acid residues, and four clones were identic al, The hexapeptides on five of the eight high affinity phage clones c ontained positively charged amino acids, identical hexapeptides were e xpressed on four of these five clones, The results of this study sugge st that the majority of the selected phages form hydrophobic and/or io nic interactions with the polymer framework rather than specific inter actions only with the yohimbine imprinted sites, Furthermore, a direct correlation can be seen between hexapeptide sequence affinity and the number of positively charged amino acid residues they contain.