Abstract
Biomimetic mineralisation of metal -organic frameworks (MOFs) is one of the most promising synthetic strategies for tailor-making MOF and hybrid bio-MOF composites which have significant potential in a variety of applications. While interactions of MOFs with several biological materials including proteins have been well studied, interactions with peptides are still relatively unexplored. Here we use phage display to identify strongly binding peptides for isoreticular MOFs (UiO-66 and UiO-66-NH2). Zeta potential and CD spectroscopy measurements combined with molecular dynamics simulations permit the characterization and explanation of the structure and dynamics of the MOF binding peptides, and differences in conformational behaviour and binding coefficients, allowing the MOF-peptide recognition mechanisms to be determined. The peptides identified through phage display have been successfully used to exert control over MOF crystallinity and particle morphology for UiO-X MOFs, from a synthesis where amorphous products form in their absence. The findings of this work have significant implications for understanding MOF-peptide interactions, which will be critical for the design and control over MOF structures and for bio-centered applications in the future.
Supplementary materials
Title
Supporting information file
Description
This file contains details of the phage display protocol and peptide analysis, materials characterisation, peptide binding (zeta potential and isothermal calorimetry), CD spectroscopy, computational details for the MD simulations, biomimetic synthesis and supplementary figures.
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