Skip to main content

This is a preprint.

It has not yet been peer reviewed by a journal.

The National Library of Medicine is running a pilot to include preprints that result from research funded by NIH in PMC and PubMed.

bioRxiv logoLink to bioRxiv
[Preprint]. 2023 Nov 2:2023.11.01.565201. [Version 1] doi: 10.1101/2023.11.01.565201

Small-molecule binding and sensing with a designed protein family

Gyu Rie Lee, Samuel J Pellock, Christoffer Norn, Doug Tischer, Justas Dauparas, Ivan Anischenko, Jaron A M Mercer, Alex Kang, Asim Bera, Hannah Nguyen, Inna Goreshnik, Dionne Vafeados, Nicole Roullier, Hannah L Han, Brian Coventry, Hugh K Haddox, David R Liu, Andy Hsien-Wei Yeh, David Baker
PMCID: PMC10635051  PMID: 37961294

Abstract

Despite transformative advances in protein design with deep learning, the design of small-molecule–binding proteins and sensors for arbitrary ligands remains a grand challenge. Here we combine deep learning and physics-based methods to generate a family of proteins with diverse and designable pocket geometries, which we employ to computationally design binders for six chemically and structurally distinct small-molecule targets. Biophysical characterization of the designed binders revealed nanomolar to low micromolar binding affinities and atomic-level design accuracy. The bound ligands are exposed at one edge of the binding pocket, enabling the de novo design of chemically induced dimerization (CID) systems; we take advantage of this to create a biosensor with nanomolar sensitivity for cortisol. Our approach provides a general method to design proteins that bind and sense small molecules for a wide range of analytical, environmental, and biomedical applications.

Full Text Availability

The license terms selected by the author(s) for this preprint version do not permit archiving in PMC. The full text is available from the preprint server.


Articles from bioRxiv are provided here courtesy of Cold Spring Harbor Laboratory Preprints

RESOURCES