Influencing bacterial S-layer protein recrystallization on polymer brushes through surface charge and accessible volume: A combined AFM and QCMD analysis

POLYMER

卷:102

Article

Moreno-Cencerrado, Alberto¹  Iturri, Jagoba¹  Pum, Dietmar¹  Sleytr, Uwe B.¹  Toca-Herrera, Jose L.¹ 

[1] Univ Nat Resources & Life Sci Vienna BOKU, Inst Biophys, Dept Nanobiotechnol, Muthgasse 11, A-1190 Vienna, Austria

关键词: Atomic force microscopy;    Quartz crystal microbalance with dissipation monitoring;    S-layer;    Self-assembly;    Polymer brushes;   

DOI  :  10.1016/j.polymer.2016.03.039

来源: Elsevier

【 摘 要 】

S-layer recrystallization is part of, at least, two major scientific and technological challenges: a model system to study 2-D polymer crystal formation and a bottom-up approach to build biomimetic and functional interfaces. In particular, the self-assembly process of the bacterial surface layer protein (SbpA) might be influenced by two different interactions: protein/substrate and protein/protein. In this work, we are taking advantage of the versatility of already well known polymer brushes to study the self-assembly mechanism of the S-protein SbpA. In particular, the recrystallization pathway of the protein has been modified by the underlying polymer charge and accessible volume offered by the positively charged poly {[2-(methacryloyloxy) ethyl] trimethylammonium chloride} (PMETAC), the negative poly(sulfo propyl methacrylate) (PSPM) and the non-charged poly(N -isopropyl acrylamide) (PNIPAAm). The recrystallization pathways on polymer brushes have been compared with the bacterial biomimetic case represented by the secondary cell wall polymer (SCWP). Results concerning protein adsorption kinetics, viscoelastic properties, crystal lattice parameters and domain formation are presented, and have been obtained with Quartz Crystal Microbalance with Dissipation Monitoring (QCMD) and Atomic Force Microscopy (AFM). (C) 2016 Elsevier Ltd. All rights reserved.

【 授权许可】

Free