[+]These authors contributed equally to this work.
Modulation of Biointeractions by Electrically Switchable Oligopeptide Surfaces: Structural Requirements and Mechanism
Article first published online: 25 JAN 2014
© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Advanced Materials Interfaces
Volume 1, Issue 2, April, 2014
How to Cite
2014). Modulation of Biointeractions by Electrically Switchable Oligopeptide Surfaces: Structural Requirements and Mechanism. Adv. Mater. Interfaces, 1: 1300085. doi: 10.1002/admi.201300085, , , , , , , , (
- Issue published online: 15 APR 2014
- Article first published online: 25 JAN 2014
- Manuscript Revised: 1 DEC 2013
- Manuscript Received: 28 OCT 2013
- Wellcome Trust. Grant Number: WT091285MA
- European Commission. Grant Number: 263091
- European Regional Development Fund (ERDF)
- switchable surfaces;
- self-assembled monolayers;
- surface plasmon resonance;
- molecular dynamic simulations
Understanding the dynamic behavior of switchable surfaces is of paramount importance for the development of controllable and tailor-made surface materials. Herein, electrically switchable mixed self-assembled monolayers based on oligopeptides have been investigated in order to elucidate their conformational mechanism and structural requirements for the regulation of biomolecular interactions between proteins and ligands appended to the end of surface tethered oligopeptides. The interaction of the neutravidin protein to a surface appended biotin ligand was chosen as a model system. All the considerable experimental data, taken together with detailed computational work, support a switching mechanism in which biomolecular interactions are controlled by conformational changes between fully extended (“ON” state) and collapsed (“OFF” state) oligopeptide conformer structures. In the fully extended conformation, the biotin appended to the oligopeptide is largely free from steric factors allowing it to efficiently bind to the neutravidin from solution. While under a collapsed conformation, the ligand presented at the surface is partially embedded in the second component of the mixed SAM, and thus sterically shielded and inaccessible for neutravidin binding. Steric hindrances aroused from the neighboring surface-confined oligopeptide chains exert a great influence over the conformational behaviour of the oligopeptides, and as a consequence, over the switching efficiency. Our results also highlight the role of oligopeptide length in controlling binding switching efficiency. This study lays the foundation for designing and constructing dynamic surface materials with novel biological functions and capabilities, enabling their utilization in a wide variety of biological and medical applications.