ENZYMATIC-HYDROLYSIS OF MULTICOMPONENT RANDOM COPOLYPEPTIDES INVITRO

Multi-component random copolypeptides membranes consisting of L-cystein (C), L-alanine (A), and L-glutamic acid (G), were synthesized by N-carboxy-amino acid anhydride (NCA) method following deblocking of the protective units of side chains by hydrogen fluoride (HF) treatment. All the water soluble samples were found extensively degraded by random chain fracture with papain. Degradation data for these samples followed the Michaelis-Menten rate law, being of the first order to the enzyme concentration. Hydrogels were prepared by intermolecular crosslinking between L-cystein residues (cystine bonding). The swelling ratio and enzymatic degradation behavior of these hydrogels were investigated in a pseudo-extracellular fluid (PECF) at pH 7.4 and 37-degrees-C as a function of copolymer composition to simulate in vivo polymer degradation. The rate of enzymatic hydolysis of hydrogels was highly dependent on the swelling ratios of the samples.