Sidechain control of porosity closure in multiple peptide-based porous materials by cooperative folding

Martí-Gastaldo, Carlos, Antypov, Dmytro, Warren, John, Briggs, Michael, Chater, Philip A., Wiper, Paul V., Miller, Gordon J., Khimyak, Yaroslav ORCID: https://orcid.org/0000-0003-0424-4128, Darling, George R., Berry, Neil G. and Rosseinsky, Matthew J. (2014) Sidechain control of porosity closure in multiple peptide-based porous materials by cooperative folding. Nature Chemistry, 6 (4). pp. 343-351. ISSN 1755-4330

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Abstract

Porous materials find application in separation, storage and catalysis. We report a crystalline porous solid formed by coordination of metal centres with a glycylserine dipeptide. We prove experimentally that the structure evolves from a solvated porous into a non-porous state as result of ordered displacive and conformational changes of the peptide that suppress the void space in response to environmental pressure. This cooperative closure, which recalls the folding of proteins, retains order in three-dimensions and is driven by the hydroxyl groups acting as H-bond donors in the peptide sequence through the serine residue. This ordered closure is also displayed by multipeptide solid solutions in which the combination of different sequences of amino acids controls their guest response in a non-linear way. This functional control can be compared to the effect of single point mutations in proteins, where the exchange of single amino acids can radically alter structure and function

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Pharmacy (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Drug Delivery and Pharmaceutical Materials (former - to 2017) Faculty of Science > Research Groups > Pharmaceutical Materials and Soft Matter
Depositing User:	Pure Connector
Date Deposited:	23 Dec 2015 12:44
Last Modified:	16 Dec 2024 01:23
URI:	https://ueaeprints.uea.ac.uk/id/eprint/55878
DOI:	10.1038/NCHEM.1871

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