Atomic Details of Carbon-Based Nanomolecules Interacting with Proteins

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ID: 110991
2020
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Abstract
Since the discovery of fullerene, carbon-based nanomolecules sparked a wealth of research across biological, medical and material sciences. Understanding the interactions of these materials with biological samples at the atomic level is crucial for improving the applications of nanomolecules and address safety aspects concerning their use in medicine. Protein crystallography provides the interface view between proteins and carbon-based nanomolecules. We review forefront structural studies of nanomolecules interacting with proteins and the mechanism underlying these interactions. We provide a systematic analysis of approaches used to select proteins interacting with carbon-based nanomolecules explored from the worldwide Protein Data Bank (wwPDB) and scientific literature. The analysis of van der Waals interactions from available data provides important aspects of interactions between proteins and nanomolecules with implications on functional consequences. Carbon-based nanomolecules modulate protein surface electrostatic and, by forming ordered clusters, could modify protein quaternary structures. Lessons learned from structural studies are exemplary and will guide new projects for bioimaging tools, tuning of intrinsically disordered proteins, and design assembly of precise hybrid materials.
Reference Key
costanzo2020moleculesatomic Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Luigi Di Costanzo;Silvano Geremia;Di Costanzo, Luigi;Geremia, Silvano;
Journal molecules
Year 2020
DOI
10.3390/molecules25153555
URL
https://www.mdpi.com/1420-3049/25/15/3555
Keywords
porous structure fullerene cyclodextrin calixarene protein crystallography macromolecules 129xe-cryptophane cucurbituril molecular tweezer nanomolecules

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