Binding characteristics between polyethylene glycol (PEG) and proteins in aqueous solution

• DOI: 10.1039/c4tb00253a
• Publication Date: 2014-03-18T12:34:27Z
• Authors: Jiang Wu; Chao Zhao; Weifeng Lin; Rundong Hu; Qiuming Wang; Hong Chen; Lingyan Li; Shengfu Chen; Jie Zheng
• Keywords: 02 engineering and technology; 0210 nano-technology; 01 natural sciences; 0104 chemical sciences; 3. Good health

Polymer-protein interactions are crucial for determining the activity of both polymer and protein many bio-related applications. Poly(ethylene glycol) (PEG) as a well-known antifouling material is often coated on surfaces to form highly solvated brushes, which exhibit excellent protein-repellent properties. However, unlike surface-induced effects, little known about intrinsic PEG-protein in aqueous solution, an important yet neglected problem. Here, we investigate between PEG proteins solution using fluorescence spectroscopy, atomic force microscopy (AFM), nuclear magnetic resonance (NMR). Two characteristics, molecular weight mass ratio : protein, examined determine effect each well binding characteristics proteins. In contrast too long short chains, collective results have shown that with optimal (MW) more capable interacting proteins, induces conformational change through stable sites stronger chain PEG. Enhanced likely due hydrophilicity amphiphilicity increasing MWPEG. almost none or weak this work provides new evidence demonstrate existence not only better understanding structure-activity relationship surfaces, but also rational design PEG-based materials specific