PerspectiveChemistry

Opening the Door to Peptide-Based Porous Solids

Science  27 Aug 2010:
Vol. 329, Issue 5995, pp. 1025-1026
DOI: 10.1126/science.1195176

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Summary

Enzymes and ion channels often undergo structural transitions that accommodate the binding of small molecules or ions, whereas porous solids that adsorb and store gases tend to have rigid structures that are unaffected by molecular binding. On page 1053 of this issue, Rabone et al. (1) describe a metal-organic framework, or MOF, made up of zinc ions bridged by flexible dipeptide linkers (glycylalanine), that changes the geometry and connectivity of its pore structure when it takes up small molecules. Unlike most porous solids, in which gas uptake increases steadily with increasing gas pressure, the gas pressure must exceed a critical “gate opening” pressure before the micropores of their material open to allow gas adsorption (see the figure, panel A). Although gating phenomena have been reported (2, 3), Rabone et al. have used an unprecedented array of experimental and computational techniques to reveal the underlying mechanism, and show that pore opening results from torsional motion and displacements of the dipeptide linkers.

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