Article Metrics


Online attention

Biomacromolecular charge chirality detected using chiral plasmonic nanostructures

DOI: 10.1039/C9NH00525K DOI Help

Authors: Marion Rodier (University of Glasgow) , Chantal Keijzer (University of Glasgow) , Joel Milner (University of Glasgow) , Affar S. Karimullah (University of Glasgow) , Aleksander W. Roszak (University of Glasgow) , Laurence D. Barron (University of Glasgow) , Nikolaj Gadegaard (University of Glasgow) , Adrian J. Lapthorn (University of Glasgow) , Malcolm Kadodwala (University of Glasgow)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nanoscale Horizons , VOL 45

State: Published (Approved)
Published: October 2019
Diamond Proposal Number(s): 16258 , 16258

Open Access Open Access

Abstract: The charge distributions of solvent exposed surfaces of complex biomolecules such has proteins are unique fingerprints. The chirality of these charge distributions result in stereo-specific electrostatic interactions which help define how proteins interact with each other, contributing to specificity in protein–protein interactions. Thus it is a key concept in understanding chemical processes in biology. There is currently no known spectroscopic phenomenon that allows rapid characterisation of chiral surface charge distributions. We show that this essential property that is currently “invisible” to optical spectroscopy, can be detected by monitoring asymmetries in the chiroptical response of protein–plasmonic nanostructure complexes. The unique capabilities of the phenomenon are utilised to discriminate between a structurally homologous series of proteins, type II dehydroquinase (DHQase) derived from different organisms. The proteins are indistinguishable with conventional structurally sensitive spectroscopy (i.e. circular dichroism). We show that discrimination between proteins can be achieved by detecting differences in chiral surface charge distributions. The phenomenon is explained with a simple model whereby the chiroptical properties of the plasmonic structures are perturbed by the induction of an enantiomeric mirror image charge distribution of the protein in the metal. This new phenomenon has broad impact, it is a powerful tool for discriminating between structurally homologous biomaterials, but will also provide information relevant to macromolecular interactions.

Subject Areas: Chemistry

Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)