Citation: Jin Li, Wen-wen Wang, Li-qiang Chu. Self-assembly of Protein-Polymer Conjugate on Gold Surface Studied by Surface Plasmon Resonance Spectroscopy[J]. Acta Polymerica Sinica, ;2018, 0(10): 1328-1335. doi: 10.11777/j.issn1000-3304.2018.18063 shu

Self-assembly of Protein-Polymer Conjugate on Gold Surface Studied by Surface Plasmon Resonance Spectroscopy

College of Chemical Engineering and Materials Science, Tianjin University of Science & Technology, Tianjin 300457

Corresponding author: Li-qiang Chu, chuliqiang@tust.edu.cn
Received Date: 13 February 2018
Revised Date: 29 March 2018
Available Online: 6 September 2018

Recently, protein-polymer conjugates, which combine protein molecules with one or more specific polymer chains at certain position, have attracted a great deal of attention due to their unique properties of both the proteins and the polymers. Therefore, the objective of this work is to study the self-assembly behavior of protein-polymer conjugates on a planar gold substrate, in which bovine serum albumin (BSA) is employed as the anchoring point for self-assembly process. We first prepare an initiator, 2-bromo-2-methylpropionic acid-2-aminooxy ethyl ester (ABM), which can be linked to the N-terminal of BSA modified by pyridoxal-5-phosphate (PLP), giving rise to a macroinitiator (i.e., BSA-Br). Then BSA-POEGMA conjugate is obtained by atom transfer radical polymerization (ATRP) using oligo(ethylene glycol) methacrylate (OEGMA) as monomer and the BSA-Br as macroinitiator, respectively. All products are characterized by Fourier-transform infrared spectroscopy (FTIR), ultraviolet-visible spectroscopy (UV-Vis) and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF-MS). FTIR and MALDI-TOF-MS results indicate that one POEGMA chain with a polymerization degree of 218 is coupled to the N-terminal of BSA. The adsorption behaviors of both the BSA and the BSA-POEGMA conjugate on gold surfaces are studied by using surface plasmon resonance spectroscopy (SPR). The data suggest that the BSA-POEGMA conjugate could be adsorbed to the gold substrate at the same way as the pure BSA molecule as expected, while the hydrophilic POEGMA chain is directed to the opposite of gold surface. At last, the adsorption behaviors of two model proteins (i.e., lysozyme, Lys and fibrinogen, Fib) on the BSA-POEGMA conjugate are also investigated. SPR data indicate that there is a decrease in Lys adsorption on the BSA-POEGMA compared to pure BSA layer. In contrast, Fib adsorption on the BSA-POEGMA conjugate increase slightly in comparison with that on pure BSA. The results clearly show the influence of POEGMA chain on the surface property of BSA molecule, which may be attributed to the water layer associated with the POEGMA chains.
- Protein-polymer conjugate,
- Bovine serum albumin,
- Poly(oligo(ethylene glycol) methacrylate),
- Surface plasmon resonance
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