Abstract
AbstractMinimalistic peptides are attractive as components for the design of active bio‐inspired materials that perform their functions enabled by the continuous turnover of chemical fuels. The first requirement for such systems is chemical complexation with the fuel source. Herein, we demonstrate the unbiased screening for heptapeptides that recognize adenosine triphosphate (ATP), life‘s ubiquitous energy source, using the in vitro method phage display. Characterization of the identified lead sequence by NMR spectroscopy and molecular dynamics simulations revealed peptide‐ATP complexes that are highly dynamic and take on an ensemble of conformations. Systematic investigation of Ala variants of the identified peptide revealed the contribution of individual residues to association with the nucleotide. Importantly, the identified heptapeptide sequence is not related to any known nucleotide‐binding motif. Our results demonstrate the application of phage display for de novo selection of short peptides that adapt their conformational space through recognition of a small molecule and provides a first step toward the design of peptide‐based ATP‐metabolizing structures.
Published Version (
Free)
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call