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Creating protein-imprinted self-assembled monolayers with multiple binding sites and biocompatible imprinted cavities
Xianfeng Zhang1, Xuezhong Du, Xuan Huang
1Key Laboratory of Mesoscopic Chemistry (Ministry of Education), and School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210093, People's Republic of China.
Journal of the American Chemical Society
|June 14, 2013
Summary
Researchers developed protein-imprinted self-assembled monolayers (SAMs) with biocompatible cavities. These SAMs demonstrate specific protein binding, offering potential for advanced biomaterials and biosensor development.
Area of Science:
- Biomaterials Science
- Surface Chemistry
- Nanotechnology
Background:
- Imprinted polymers offer advantages over bulk materials, including enhanced mass transfer and real-time signal detection.
- Protein-imprinted self-assembled monolayers (SAMs) are a promising platform for specific molecular recognition.
Purpose of the Study:
- To create protein-imprinted SAMs with multiple, biocompatible binding sites.
- To investigate the role of a novel disulfide compound (DHAP) in forming these imprinted cavities.
- To evaluate the specific protein-binding capabilities of the developed SAMs.
Main Methods:
- Fabrication of protein-imprinted SAMs using functional thiols and a novel disulfide compound (DHAP) in a benign solution.
- Incorporation of oligoethylene glycol (OEG) terminal moiety and amide groups within DHAP.
- Characterization of binding sites and cavities, and assessment of nonspecific protein binding.
Main Results:
- The developed SAMs featured multiple binding sites and biocompatible cavities.
- DHAP effectively contributed to cavity formation and resisted nonspecific protein binding.
- The protein-imprinted SAMs demonstrated excellent specific binding of target proteins.
Conclusions:
- The strategy enables the creation of tailor-made monolayer surfaces for specific protein recognition.
- This approach facilitates the controlled assembly of biomaterials.
- The developed SAMs show potential for the preparation of advanced biosensors.
