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Tuning Protein Frameworks via Auxiliary Supramolecular Interactions. | LitMetric

Tuning Protein Frameworks via Auxiliary Supramolecular Interactions.

ACS Nano

School of Chemistry , National University of Ireland Galway , University Road, Galway H91 TK33 , Ireland.

Published: September 2019

Protein crystals with their precise, periodic array of functional building blocks have potential applications in biomaterials, sensing, and catalysis. This paper describes how a highly porous crystalline framework of a cationic redox protein and an anionic macrocycle can be modulated by a small cationic effector. Ternary composites of protein (∼13 kDa), calix[8]arene (∼1.5 kDa), and effector (∼0.2 kDa) formed distinct crystalline architectures, dependent on the effector concentration and the crystallization technique. A combination of X-ray crystallography and density functional theory (DFT) calculations was used to decipher the framework variations, which appear to be dependent on a calixarene conformation change mediated by the effector. This "switch" calixarene was observed in three states, each of which is associated with a different interaction network. Two structures obtained by co-crystallization with the effector contained an additional protein "pillar", resulting in framework duplication and decreased porosity. These results suggest how protein assembly can be engineered by supramolecular host-guest interactions.

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Source
http://dx.doi.org/10.1021/acsnano.9b04115DOI Listing

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