Next Article in Journal
Isolation and Purification of Potent Growth Inhibitors from Piper methysticum Root
Next Article in Special Issue
Instrumentation for Vibrational Circular Dichroism Spectroscopy: Method Comparison and Newer Developments
Previous Article in Journal
Description of a Naphthoquinonic Crystal Produced by the Fungus Scytalidium cuboideum
Previous Article in Special Issue
Circular Dichroism in Fluorescence Emission Following the C 1s→π* Excitation and Resonant Auger Decay of Carbon Monoxide
Article Menu
Issue 8 (August) cover image

Export Article

Open AccessReview
Molecules 2018, 23(8), 1906; https://doi.org/10.3390/molecules23081906

UV-Denaturation Assay to Assess Protein Photostability and Ligand-Binding Interactions Using the High Photon Flux of Diamond B23 Beamline for SRCD

B23 Beamline, Diamond Light Source, Harwell Science Innovation Campus, Chilton, Didcot OX11 0DE, UK
*
Authors to whom correspondence should be addressed.
Received: 8 June 2018 / Revised: 10 July 2018 / Accepted: 10 July 2018 / Published: 31 July 2018
(This article belongs to the Special Issue Recent Advances in Chiroptical Spectroscopy)
Full-Text   |   PDF [2216 KB, uploaded 24 August 2018]   |  

Abstract

Light irradiation with high photon flux in the vacuum and far-UV region is known to denature the conformation of biopolymers. Measures are in place at Diamond Light Source B23 beamline for Synchrotron Radiation Circular Dichroism (SRCD) to control and make this effect negligible. However, UV denaturation of proteins can also be exploited as a novel method for assessing biopolymer photostability as well as ligand-binding interactions. Usually, host–ligand binding interactions can be assessed monitoring CD changes of the host biopolymer upon ligand addition. The novel method of identifying ligand binding monitoring the change of relative rate of UV denaturation using SRCD is especially important when there are very little or insignificant secondary structure changes of the host protein upon ligand binding. The temperature study, another method used to determine molecular interactions, can often be inconclusive when the thermal effect associated with the displacement of the bound solvent molecules by the ligand is also small, making the determination of the binding interaction inconclusive. Herein we present a review on the UV-denaturation assay as a novel method to determine the relative photostability of protein formulations as well as the screening of ligand-binding interactions using the high photon flux Diamond B23 beamline for SRCD. View Full-Text
Keywords: circular dichroism; ligand binding; high photon flux; protein stability; synchrotron radiation; SRCD; vacuum UV circular dichroism; ligand binding; high photon flux; protein stability; synchrotron radiation; SRCD; vacuum UV
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Hussain, R.; Longo, E.; Siligardi, G. UV-Denaturation Assay to Assess Protein Photostability and Ligand-Binding Interactions Using the High Photon Flux of Diamond B23 Beamline for SRCD. Molecules 2018, 23, 1906.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top