Biodegradation of copoly(n-hydroxypropyl- d,l-glutamine) in vitro

• Published in: European polymer journal Vol. 30; no. 9; pp. 1065 - 1069
• Main Authors: Hayashi, Toshio, Nakanishi, Eiji, Iizuka, Yasuko, Oya, Masanao, Iwatsuki, Makoto
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01.09.1994; Elsevier
• Subjects: Aminoacid polymers; Applied sciences; Exact sciences and technology; Physicochemistry of polymers; Synthetic biopolymers; Chemical solution; Property composition relationship; Enzyme; Biodegradability; Cysteine endopeptidases; Intrinsic viscosity; Aminoacid copolymer; Papain; Experimental study; In vitro; Molecular weight property relation; Random copolymer; Chemical modification; Aminolysis; Preparation; Enzymatic digestion; Hydrolases; Property structure relationship; Kinetics; Proteinases; Glutamic acid derivative copolymer
• ISSN: 0014-3057; 1873-1945
• DOI: 10.1016/0014-3057(94)90201-1

Random copolypeptides (PHPDLG) consisting of N-hydroxypropyl- d-glutamine (HPDG) and N-hydroxypropyl- l-glutamine (HPLG) covering the whole range of d,l-copolymer composition were prepared by carrying out aminolysis reactions with 3-amino-1-propanol (P) on starting random copolymers consisting of γ-benzyl- d-glutamate and γ-benzyl- l-glutamate (PBDLG). The effects of copolymer composition and sequential distributions on the rate of hydrolysis by papain in a pseudo-extracellular fluid (PECF) at pH 7.4 and 37.0°C were studied to simulate in vivo polymer degradation. Degradation data for these samples followed the Michaelis-Menten rate law, being of the first order to the enzyme concentration. It was shown that the rate of degradation by papain was controlled by the comonomer composition as well as sequential distributions of comonomers in the copolymer chains.