Terpolymerization kinetics of amino acid N‐carboxy anhydrides. Issue 9 (12th February 2014)

• Record Type: Journal Article
• Authors: Zelzer, Mischa; Heise, Andreas
• Is Part Of: Journal of polymer science. Volume 52:Issue 9(2014:May)
• Page Start: 1228
• Page End: 1236
• Publication Date: 2014-02-12
• Subjects: copolymerization -- glutamic acid -- lysine -- polymerization kinetics -- polypeptides -- tyrosine; 547
• DOI: 10.1002/pola.27109
• Languages: English
• ISSNs: 0887-624X

Abstract

ABSTRACT: Based on their versatility with respect to amino acid type and sequence, polypeptides have become attractive for a number of biological applications such as drug delivery, biomineralization, and drugs. N‐carboxy anhydride (NCA) polymerization is a convenient way to rapidly prepare high‐molecular weight polypeptides with good control over molecular weight and polydispersity. However, the kinetics of the incorporation of NCA monomers into copolypeptides during random copolymerization are poorly understood. Here, kinetic data is presented that allows insight into the NCA polymerization of a terpolymer composed of three commercially relevant amino acids, namely, glutamic acid, lysine, and tyrosine. Furthermore, kinetic data and copolymerization parameters from the copolymerization of binary mixtures of these three amino acid NCAs is used to make predictions of the terpolymer composition. This study provides access to the information necessary to prepare functional copolypeptides with better‐defined sequence architecture that will be essential for the future development of polypeptide‐based materials. © 2014 Wiley Periodicals, Inc. J. Polym. Sci., Part A: Polym. Chem. 2014, 52, 1228–1236 Abstract : The polymerization kinetics of the reaction of three N‐carboxy anhydrides (NCA), Glu(Bzl)‐NCA, Lys(Z)‐NCA, and Tyr(Bzl)‐NCA in a random copolymerization are determined using a recently developed high‐performance liquid chromatography (HPLC)‐based approach. Monomer consumption over time can be followed during the terpolymerization, and the relative reactivity of the monomers can be determined. The kinetic data is further used to deduce information about the composition of the final polypeptide.