Jump to main content
Jump to site search


A medium-firm drug-candidate library of cryptand-like structures on T7 phage: design and selection of a strong binder for Hsp90

Author affiliations

Abstract

We designed and synthesized a medium-firm drug-candidate library of cryptand-like structures possessing a randomized peptide linker on the bacteriophage T7. From the macrocyclic library with a 109 diversity, we obtained a binder toward a cancer-related protein (Hsp90) with an antibody-like strong affinity (KD = 62 nM) and the binding was driven by the enthalpy. The selected supramolecular ligand inhibited Hsp90 activity by site-specific binding outside of the well-known ATP-binding pocket on the N-terminal domain (NTD).

Graphical abstract: A medium-firm drug-candidate library of cryptand-like structures on T7 phage: design and selection of a strong binder for Hsp90

Back to tab navigation

Supplementary files

Article information


Submitted
08 Sep 2020
Accepted
12 Oct 2020
First published
14 Oct 2020

Org. Biomol. Chem., 2020, Advance Article
Article type
Communication

A medium-firm drug-candidate library of cryptand-like structures on T7 phage: design and selection of a strong binder for Hsp90

K. Mochizuki, L. Matsukura, Y. Ito, N. Miyashita and M. Taki, Org. Biomol. Chem., 2020, Advance Article , DOI: 10.1039/D0OB01855D

Social activity

Search articles by author

Spotlight

Advertisements