ReviewMolecules (Basel, Switzerland)2018
UV-Denaturation Assay to Assess Protein Photostability and Ligand-Binding Interactions Using the High Photon Flux of Diamond B23 Beamline for SRCD.
Review in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Enzyme-Ligand Interaction Monitored by Synchrotron Radiation Circular Dichroism.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Enhanced Protein Photo-Stability Analysis Using SRCD in the Presence of Phospholipid SUVs.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Analytical approaches for assessing protein structure in protein-rich food: A comprehensive review.Food chemistry: X · 2024Review
- Interaction of Blenoxane and Congeners Bleomycins A2 and B2 with Human Plasma Proteins Using Circular Dichroism Spectroscopy.International journal of molecular sciences · 2023Article
- Free Radical Generation in Far-UV Synchrotron Radiation Circular Dichroism Assays-Protein and Buffer Composition Contribution.International journal of molecular sciences · 2021Article
- Interaction of a Short Peptide with G-Quadruplex-Forming Sequences: An SRCD and CD Study.Pharmaceutics · 2021Article
- The Secondary Structure of a Major Wine Protein is Modified upon Interaction with Polyphenols.Molecules (Basel, Switzerland) · 2020Article
- Application of Circular Dichroism and Fluorescence Spectroscopies To Assess Photostability of Water-Soluble Porcine Lens Proteins.ACS omega · 2020Article
- Characterisation of sensor kinase by CD spectroscopy: golden rules and tips.Biochemical Society transactions · 2018Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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