The facile synthesis of an aldehyde-containing graft copolymer membrane for covalent protein capture with retention of protein functionality

• Published in: Journal of Chromatography A Vol. 1217; no. 12; pp. 1904 - 1911
• Main Authors: Yong, Joel K.J., Xiao, Youchang, Chung, Tai-Shung
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 19.03.2010
• Subjects: Adsorption; Aldehydes - chemistry; Animals; Atom transfer radical polymerization; bovine serum albumin; Cattle; Chemistry Techniques, Analytical - methods; chromatography; Chromatography, Gel; composite polymers; Hydrogen-Ion Concentration; Kinetics; longevity; Membrane chromatography; Membranes, Artificial; Microscopy, Electron, Scanning; Photoelectron Spectroscopy; polymerization; Polymers - chemical synthesis; Polyvinyls; Porosity; Protein adsorption; Serum Albumin, Bovine - isolation & purification; Stereoisomerism; synthesis; temperature; Time Factors; tryptophan; Tryptophan - chemistry; Tryptophan enantioresolution; Atom transfer radical polymerization; Membrane chromatography; Protein adsorption; Tryptophan enantioresolution
• ISSN: 0021-9673; 1873-3778
• DOI: 10.1016/j.chroma.2010.01.051

The immobilization of biomolecules onto an insoluble carrier surface has always been a subject of great interest to enhance their resistance to pH and temperature, which aids in an increased activity lifespan as well as easy reuse of the said biomolecules. However, traditional methods are only able to provide single-layer biomolecular binding and require multiple chemical reactions to prepare the final substrate before the immobilization can be carried out properly. Here we report a facile one-step chemical synthesis of a new aldehyde-bearing graft copolymer via atom transfer radical polymerization (ATRP) for covalent protein capture in a multilayered approach to covalently capture bovine serum albumin (BSA) onto a polymeric membrane. The resultant protein-bound membrane illustrated the retention of BSA's stereoselective discrimination ability by binding to an excess of 2 mol of tryptophan/mol of BSA and demonstrated an enantioresolution of a 0.184 mM racemic tryptophan mixture with a time-averaged-separation factor of 2.9.