Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/102086
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Type: | Journal article |
Title: | The key position: influence of staple location on constrained peptide conformation and binding |
Author: | Keeling, K. Cho, O. Scanlon, D. Booker, G. Abell, A. Wegener, K. |
Citation: | Organic and Biomolecular Chemistry, 2016; 14(41):9731-9735 |
Publisher: | The Royal Society of Chemistry |
Issue Date: | 2016 |
ISSN: | 1477-0520 1477-0539 |
Statement of Responsibility: | Kelly L. Keeling, Okki Cho, Denis B. Scanlon, Grant W. Booker, Andrew D. Abell and Kate L. Wegener |
Abstract: | Constrained α-helical peptides are showing potential as biological probes and therapeutic agents that target protein-protein interactions. However, the factors that determine the optimal constraint locations are still largely unknown. Using the β-integrin/talin protein interaction as a model system, we examine the effect of constraint location on helical conformation, as well as binding affinity, using circular dichroism and NMR spectroscopy. Stapling increased the overall helical content of each integrin-based peptide tested. However, NMR analysis revealed that different regions within the peptide are stabilised, depending on constraint location, and that these differences correlate with the changes observed in talin binding mode and affinity. In addition, we show that examination of the atomic structure of the parent peptide provides insight into the appropriate placement of helical constraints. |
Keywords: | Lactams Peptide Fragments Talin Integrin beta3 Amino Acid Sequence Protein Structure, Secondary Protein Binding Models, Molecular Proteolysis |
Description: | First published online 29 Sep 2016 |
Rights: | This journal is © The Royal Society of Chemistry 2016 |
DOI: | 10.1039/c6ob01745b |
Grant ID: | http://purl.org/au-research/grants/arc/DP120100582 |
Published version: | http://dx.doi.org/10.1039/c6ob01745b |
Appears in Collections: | Aurora harvest 7 Molecular and Biomedical Science publications |
Files in This Item:
File | Description | Size | Format | |
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hdl_102086.pdf | Accepted Version | 8.27 MB | Adobe PDF | View/Open |
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