Surface-Mediated Supramolecular Self-Assembly of Protein, Peptide, and Nucleoside Derivatives: From Surface Design to the Underlying Mechanism and Tailored Functions

Yang, Bin; Adams, Dave J.; Marlow, Maria; Zelzer, Mischa

Abstract

Among the many parameters that have been explored to exercise control over self-assembly processes, the influence of surface properties on self-assembly has been recognized as important but has received considerably less attention than other factors. This is particularly true for biomolecule-derived self-assembling molecules such as protein, peptide, and nucleobase derivatives. Because of their relevance to biomaterial and drug delivery applications, interest in these materials is increasing. As the formation of supramolecular structures from these biomolecule derivatives inevitably brings them into contact with the surfaces of surrounding materials, understanding and controlling the impact of the properties of these surfaces on the self-assembly process are important. In this feature article, we present an overview of the different surface parameters that have been used and studied for the direction of the self-assembly of protein, peptide, and nucleoside-based molecules. The current mechanistic understanding of these processes will be discussed, and potential applications of surface-mediated self-assembly will be outlined.

Citation

Yang, B., Adams, D. J., Marlow, M., & Zelzer, M. (2018). Surface-Mediated Supramolecular Self-Assembly of Protein, Peptide, and Nucleoside Derivatives: From Surface Design to the Underlying Mechanism and Tailored Functions. Langmuir, 34(50), 15109-15125. https://doi.org/10.1021/acs.langmuir.8b01165

• Journal Article Type: Article
• Acceptance Date: Jul 21, 2018
• Online Publication Date: Jul 21, 2018
• Publication Date: Dec 18, 2018
• Deposit Date: Apr 30, 2019
• Publicly Available Date: May 15, 2019
• Journal: Langmuir
• Print ISSN: 0743-7463
• Electronic ISSN: 1520-5827
• Publisher: American Chemical Society
• Peer Reviewed: Peer Reviewed
• Volume: 34
• Issue: 50
• Pages: 15109-15125
• DOI: https://doi.org/10.1021/acs.langmuir.8b01165
• Public URL: https://nottingham-repository.worktribe.com/output/1871238
• Publisher URL: https://pubs.acs.org/doi/10.1021/acs.langmuir.8b01165