| Literature DB >> 29316089 |
Adam J Gormley1, Jonathan Yeow2,3, Gervase Ng2,3, Órla Conway2,4, Cyrille Boyer2,3, Robert Chapman2,4.
Abstract
The complexity of polymer-protein interactions makes rational design of the best polymer architecture for any given biointerface extremely challenging, and the high throughput synthesis and screening of polymers has emerged as an attractive alternative. A porphyrin-catalysed photoinduced electron/energy transfer-reversible addition-fragmentation chain-transfer (PET-RAFT) polymerisation was adapted to enable high throughput synthesis of complex polymer architectures in dimethyl sulfoxide (DMSO) on low-volume well plates in the presence of air. The polymerisation system shows remarkable oxygen tolerance, and excellent control of functional 3- and 4-arm star polymers. We then apply this method to investigate the effect of polymer structure on protein binding, in this case to the lectin concanavalin A (ConA). Such an approach could be applied to screen the structure-activity relationships for any number of polymer-protein interactions.Entities:
Keywords: PET-RAFT; click chemistry; glycopolymers; oxygen tolerance; photomediated radical polymerization
Year: 2018 PMID: 29316089 DOI: 10.1002/anie.201711044
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336