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Abstract
Polyamides derived from the tyrosine-leucine (Tyr-Leu) peptide bond were prepared using monomers synthesized via the diphenyl phosphoryl azide (DPPA) coupling method. Spacers of varying chain lengths and functionalities were incorporated between the Tyr-Leu dipeptide. The spacers reported here include poly(oxypropylenediamine) (Jeffamine), and dodecanediamine. The Jeffamine-containing polymers, synthesized by polycondensation with sebacoyl chloride in DMF and chloroform, were found to have an M w/M n of 47,600/26,700 and 32,000/ 23,700, respectively. The polymers derived from the dodecanediamine spacer and sebacoyl chloride gave a polymer with M w/M n of 47,000/ 26,000 as determined by GPC analysis. In another experiment, poly(β-alanyltyrosylleucyl-β-alanine), a previously synthesized polyamide with M w/M n of 16,500/5,700, was subjected to enzymatic degradation targeting the Tyr-Leu dipeptide of naturally occurring L-amino acids. The proteases thermolysin, subtilisin, chymotrypsin, and aspergillopeptidase A were used. The total organic carbon (TOC) analysis method was used to determine the extent of degradation. The polymer was found to degrade with the thermolysin protease under appropriate buffer and temperature conditions.