Multivalent Calixarene Complexation of a Designed Pentameric Lectin

Research output: Contribution to a Journal (Peer & Non Peer)Articlepeer-review

8 Citations (Scopus)

Abstract

We describe complex formation between a designed pentameric β-propeller and the anionic macrocycle sulfonato-calix[8]arene (sclx8), as characterized by X-ray crystallography and NMR spectroscopy. Two crystal structures and 15N HSQC experiments reveal a single calixarene binding site in the concave pocket of the β-propeller toroid. Despite the symmetry mismatch between the pentameric protein and the octameric macrocycle, they form a high affinity multivalent complex, with the largest protein-calixarene interface observed to date. This system provides a platform for investigating multivalency.

Original languageEnglish
Pages (from-to)1303-1309
Number of pages7
JournalBiomacromolecules
Volume25
Issue number2
DOIs
Publication statusPublished - 12 Feb 2024

Fingerprint

Dive into the research topics of 'Multivalent Calixarene Complexation of a Designed Pentameric Lectin'. Together they form a unique fingerprint.

Cite this