The histidine residue in the peptide D-Lys6-GnRHhas been shown to co-polymerize in situ withethylcyanoacrylate (ECA). This study investigated (I) thepotential of D-Lys6-GnRH to co-polymerize with anotherpolymer (butylcyanoacrylate), and (ii) the in situpolymerization of insulin and human ACTH(adrenocorticotropic hormone) with ECA. ACTH containsno histidine and did not co-polymerize. Insulin containstwo histidine residues, but also did not co-polymerize.This might be explained by the complexity of theconformational arrangement of the molecule. Underpolymerization conditions, insulin exists in the hexamericstate, with the histidine residues being buried inside themolecule. Consequently, depending on the stericalavailability of the nucleophile, not all histidine-containingmodels will necessarily co-polymerize with PACA. Thesmall peptide D-Lys6-GnRH, however, seems to havelarge potential to interfere in the polymerization.
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