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Protein-induced modifications in crystal morphology of a hydrogen-bonded organic framework
In this work, we studied the encapsulation of a range of proteins in a hydrogen-bonded organic framework (HOF) comprised of a tetraamidinium cation and diazobenzene-based dicarboxylate anion. We explore the use of external stimuli: light and temperature to modulate HOF crystal growth and size. In pa...
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Published in: | Journal of materials chemistry. A, Materials for energy and sustainability Materials for energy and sustainability, 2023-10, Vol.11 (42), p.2326-2333 |
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container_issue | 42 |
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container_title | Journal of materials chemistry. A, Materials for energy and sustainability |
container_volume | 11 |
creator | Flint, Kate L Evans, Jack D Carraro, Francesco Renner, Simon Linder-Patton, Oliver M Amenitsch, Heinz Falconer, Robert J White, Nicholas G Sumby, Christopher J Falcaro, Paolo Doonan, Christian J |
description | In this work, we studied the encapsulation of a range of proteins in a hydrogen-bonded organic framework (HOF) comprised of a tetraamidinium cation and diazobenzene-based dicarboxylate anion. We explore the use of external stimuli: light and temperature to modulate HOF crystal growth and size. In particular, we found photo-isomerisation can be used to control the concentration of the
trans
-azobenzene building block that contributes to HOF formation. When HOF growth was slowed sufficiently, deformation of the crystals and ultimately multicrystal aggregates were observed in the presence of some proteins. We propose that the extent of crystal deformation, consistent with better protein association, may be governed by differences in the type and strength of interactions between proteins and the surface of the growing HOF crystals.
In this work, we studied the encapsulation of a range of proteins in a hydrogen-bonded organic framework (HOF) comprised of a tetraamidinium cation and diazobenzene-based dicarboxylate anion. |
doi_str_mv | 10.1039/d3ta04707e |
format | article |
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trans
-azobenzene building block that contributes to HOF formation. When HOF growth was slowed sufficiently, deformation of the crystals and ultimately multicrystal aggregates were observed in the presence of some proteins. We propose that the extent of crystal deformation, consistent with better protein association, may be governed by differences in the type and strength of interactions between proteins and the surface of the growing HOF crystals.
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trans
-azobenzene building block that contributes to HOF formation. When HOF growth was slowed sufficiently, deformation of the crystals and ultimately multicrystal aggregates were observed in the presence of some proteins. We propose that the extent of crystal deformation, consistent with better protein association, may be governed by differences in the type and strength of interactions between proteins and the surface of the growing HOF crystals.
In this work, we studied the encapsulation of a range of proteins in a hydrogen-bonded organic framework (HOF) comprised of a tetraamidinium cation and diazobenzene-based dicarboxylate anion.</description><subject>Azo compounds</subject><subject>Crystal growth</subject><subject>Crystals</subject><subject>Deformation</subject><subject>External stimuli</subject><subject>Hydrogen bonding</subject><subject>Isomerization</subject><subject>Proteins</subject><issn>2050-7488</issn><issn>2050-7496</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNpFkE1LAzEQhoMoWGov3oWAN2E1u9mP5Fhq_YCCHurFy5LNTNrUNqnJLrL_3tVKncsMvM_MwEPIZcpuU8blHfBWsbxiFZ6QUcYKllS5LE-PsxDnZBLjhg0lGCulHJH31-BbtC6xDjqNQHcerLFatda7SK2jOvSxVdshCPu13_pVT72hiq57CH6FLmm8g2HRh5VyVlMT1A6_fPi4IGdGbSNO_vqYvD3Ml7OnZPHy-DybLhKdibRNgKfARAOokJtC6EIBCqUagUKyHCVAUykjTVrmXOsCWGYATYZVpQQ0JfIxuT7c3Qf_2WFs643vghte1pkQecZllhYDdXOgdPAxBjT1PtidCn2dsvpHX33Pl9NfffMBvjrAIeoj96-XfwO3528g</recordid><startdate>20231031</startdate><enddate>20231031</enddate><creator>Flint, Kate L</creator><creator>Evans, Jack D</creator><creator>Carraro, Francesco</creator><creator>Renner, Simon</creator><creator>Linder-Patton, Oliver M</creator><creator>Amenitsch, Heinz</creator><creator>Falconer, Robert J</creator><creator>White, Nicholas G</creator><creator>Sumby, Christopher J</creator><creator>Falcaro, Paolo</creator><creator>Doonan, Christian J</creator><general>Royal Society of Chemistry</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7SP</scope><scope>7SR</scope><scope>7ST</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>JG9</scope><scope>L7M</scope><scope>SOI</scope><orcidid>https://orcid.org/0000-0002-4173-9931</orcidid><orcidid>https://orcid.org/0000-0001-5935-0409</orcidid><orcidid>https://orcid.org/0000-0003-2975-0887</orcidid><orcidid>https://orcid.org/0000-0002-9713-9599</orcidid><orcidid>https://orcid.org/0000-0001-8485-4676</orcidid><orcidid>https://orcid.org/0000-0003-2822-0956</orcidid><orcidid>https://orcid.org/0000-0001-9521-2601</orcidid><orcidid>https://orcid.org/0000-0002-9043-8369</orcidid></search><sort><creationdate>20231031</creationdate><title>Protein-induced modifications in crystal morphology of a hydrogen-bonded organic framework</title><author>Flint, Kate L ; Evans, Jack D ; Carraro, Francesco ; Renner, Simon ; Linder-Patton, Oliver M ; Amenitsch, Heinz ; Falconer, Robert J ; White, Nicholas G ; Sumby, Christopher J ; Falcaro, Paolo ; Doonan, Christian J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c281t-d31d08bdeae3f58c5ade8aab8e8904e9ddb7af9f1643cc5d02fdef2e77a8db6e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Azo compounds</topic><topic>Crystal growth</topic><topic>Crystals</topic><topic>Deformation</topic><topic>External stimuli</topic><topic>Hydrogen bonding</topic><topic>Isomerization</topic><topic>Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Flint, Kate L</creatorcontrib><creatorcontrib>Evans, Jack D</creatorcontrib><creatorcontrib>Carraro, Francesco</creatorcontrib><creatorcontrib>Renner, Simon</creatorcontrib><creatorcontrib>Linder-Patton, Oliver M</creatorcontrib><creatorcontrib>Amenitsch, Heinz</creatorcontrib><creatorcontrib>Falconer, Robert J</creatorcontrib><creatorcontrib>White, Nicholas G</creatorcontrib><creatorcontrib>Sumby, Christopher J</creatorcontrib><creatorcontrib>Falcaro, Paolo</creatorcontrib><creatorcontrib>Doonan, Christian J</creatorcontrib><collection>CrossRef</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Environment Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Environment Abstracts</collection><jtitle>Journal of materials chemistry. 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trans
-azobenzene building block that contributes to HOF formation. When HOF growth was slowed sufficiently, deformation of the crystals and ultimately multicrystal aggregates were observed in the presence of some proteins. We propose that the extent of crystal deformation, consistent with better protein association, may be governed by differences in the type and strength of interactions between proteins and the surface of the growing HOF crystals.
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subjects | Azo compounds Crystal growth Crystals Deformation External stimuli Hydrogen bonding Isomerization Proteins |
title | Protein-induced modifications in crystal morphology of a hydrogen-bonded organic framework |
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