Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/112781
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Type: Journal article
Title: Protein surface functionalisation as a general strategy for facilitating biomimetic mineralisation of ZIF-8
Author: Maddigan, N.
Tarzia, A.
Huang, D.
Sumby, C.
Bell, S.
Falcaro, P.
Doonan, C.
Citation: Chemical Science, 2018; 9(18):4217-4223
Publisher: Royal Society of Chemistry
Issue Date: 2018
ISSN: 2041-6520
2041-6539
Statement of
Responsibility: 
Natasha K. Maddigan, Andrew Tarzia, David M. Huang, Christopher J. Sumby, Stephen G. Bell, Paolo Falcaro and Christian. J. Doonan
Abstract: The durability of enzymes in harsh conditions can be enhanced by encapsulation within metal-organic frameworks (MOFs) via a process called biomimetic mineralisation. Herein we show that the surface charge and chemistry of a protein determines its ability to seed MOF growth. We demonstrate that chemical modification of amino acids on the protein surface is an effective method for systematically controlling biomimetic mineralisation by zeolitic imidazolate framework-8 (ZIF-8). Reaction of surface lysine residues with succinic (or acetic) anhydride facilitates biomimetic mineralisation by increasing the surface negative charge, whereas reaction of surface carboxylate moieties with ethylenediamine affords a more positively charged protein and hinders the process. Moreover, computational studies confirm that the surface electrostatic potential of a protein is a good indicator of its ability to induce biomimetic mineralisation. This study highlights the important role played by protein surface chemistry in encapsulation and outlines a general method for facilitating the biomimetic mineralisation of proteins.
Rights: This journal is © The Royal Society of Chemistry 2018
RMID: 0030088666
DOI: 10.1039/c8sc00825f
Grant ID: http://purl.org/au-research/grants/arc/DP170103531
Appears in Collections:Chemistry publications

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