Polymers containing enzymatically degradable bonds, 8. Degradation of oligopeptide sequences in <i>N</i>‐(2‐hydroxypropyl)methacrylamide copolymers by bovine spleen cathepsin B

Abstract

Abstract Three types of copolymers of N ‐(2‐hydroxypropyl)methacrylamide(HPMA) were prepared which contain oligopeptide sequences: (a) HPMA copolymers containing oligopeptide side‐chains terminated with p ‐nitroaniline; (b) soluble HPMA copolymers containing oligopeptide sequences in crosslinks connecting two poly(HPMA) chains; (c) a hydrophilic gel, i.e. a three dimensional copolymer of HPMA containing an oligopeptide sequence in the crosslinks. These polymeric substrates (suitable as drug carriers) containing potentially degradable oligopeptide sequences were incubated with an intracellular proteolytic enzyme, bovine spleen cathespin B. The degradation process of the substrates made it possible to reveal the relationship between the structure of oligopeptide sequences and their degradability. The results suggest an important role played by cathepsin B in the degradation of polymeric substrates investigated in this study under physiological conditions.