Binding interactions of Peptide Aptamers

New, Roger ORCID logoORCID: https://orcid.org/0000-0001-5625-7735, Bui, Tam T. T. and Bogus, Michael (2020) Binding interactions of Peptide Aptamers. Molecules, 25 (24) , 6055. pp. 1-9. ISSN 1420-3049 [Article] (doi:10.3390/molecules25246055)

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Abstract

Peptide aptamers are short amino acid chains that are capable of binding specifically to ligands in the same way as their much larger counterparts, antibodies. Ligands of therapeutic interest that can be targeted are other peptide chains or loops located on the surface of protein receptors (e.g., GCPR), which take part in cell-to-cell communications either directly or via the intermediary of hormones or signalling molecules. To confer on aptamers the same sort of conformational rigidity that characterises an antibody binding site, aptamers are often constructed in the form of cyclic peptides, on the assumption that this will encourage stronger binding interactions than would occur if the aptamers were simply linear chains. However, no formal studies have been conducted to confirm the hypothesis that linear peptides will engage in stronger binding interactions with cyclic peptides than with other linear peptides. In this study, the interaction of a model cyclic decamer with a series of linear peptide constructs was compared with that of a linear peptide with the same sequence, showing that the cyclic configuration does confer benefits by increasing the strength of binding.

Item Type: Article
Additional Information: This article belongs to the Special Issue Advances in Research of Short Peptides.
Keywords (uncontrolled): Peptide therapeutics, cyclic peptide, lipo-amino acid, hydrogen bond, fluorescence enhancement, peptide aptamer
Research Areas: A. > School of Science and Technology
Item ID: 31746
Notes on copyright: © 2020 by the authors.
Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Depositing User: Jisc Publications Router
Date Deposited: 06 Jan 2021 17:25
Last Modified: 26 Jan 2021 16:24
URI: https://eprints.mdx.ac.uk/id/eprint/31746

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