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Photoactive Biological Molecules

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Physical Chemistry".

Deadline for manuscript submissions: closed (31 December 2020) | Viewed by 2968

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Guest Editor
Department of Chemistry, University of York, Heslington, York YO10 5DD, UK
Interests: biological molecules in the gas-phase; gaseous ions; laser spectroscopy; molecular clusters; photoionization spectroscopy; computational chemistry; electron-molecule scattering; molecular anions; nucleobase photophysics; collision-induced dissociation; photodegradation
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Special Issue Information

Dear colleague,

Physical chemists are advancing our fundamental understanding of light’s role in biological systems, and are contributing to the development of new applications that embrace the photoactivity of molecules in biochemical environments. Organisms on Earth have evolved to use natural light in a wide variety of ways, from prominent examples including vision and photosynthesis, through to more subtle cases such as bioluminescence. Conversely, biomolecules such as DNA have adapted to allow the dissipation of harmful UV light that penetrates to the Earth’s surface. Understanding the photophysics and photochemistry of these processes enables physical chemists to provide important insights into the fundamental light-driven mechanisms of chemical biology, and provide key clues to allow us to develop new systems that can mimic their function for new technological examples. To celebrate the rich diversity of current work in this field of physical chemistry, our journal Molecules will launch a Special Issue on “Photoactive Biological Molecules”, to be published in 2020. We encourage the contribution of high-quality papers and review articles in all areas of physical chemistry that focus on the interaction of light and biologically relevant molecules.

Dr. Caroline Dessent
Guest Editor

Manuscript Submission Information

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Published Papers (1 paper)

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Research

18 pages, 4349 KiB  
Article
Generation and Characterization of a DNA-GCN4 Oligonucleotide-Peptide Conjugate: The Impact DNA/Protein Interactions on the Sensitization of DNA
by Paweł Wityk, Rafał Piątek, Robert Nowak and Dorota Kostrzewa-Nowak
Molecules 2020, 25(16), 3630; https://doi.org/10.3390/molecules25163630 - 10 Aug 2020
Cited by 5 | Viewed by 2569
Abstract
Radiotherapy, the most common therapy for the treatment of solid tumors, exerts its effects by inducing DNA damage. To fully understand the extent and nature of this damage, DNA models that mimic the in vivo situation should be utilized. In a cellular context, [...] Read more.
Radiotherapy, the most common therapy for the treatment of solid tumors, exerts its effects by inducing DNA damage. To fully understand the extent and nature of this damage, DNA models that mimic the in vivo situation should be utilized. In a cellular context, genomic DNA constantly interacts with proteins and these interactions could influence both the primary radical processes (triggered by ionizing radiation) and secondary reactions, ultimately leading to DNA damage. However, this is seldom addressed in the literature. In this work, we propose a general approach to tackle these shortcomings. We synthesized a protein-DNA complex that more closely represents DNA in the physiological environment than oligonucleotides solution itself, while being sufficiently simple to permit further chemical analyses. Using click chemistry, we obtained an oligonucleotide-peptide conjugate, which, if annealed with the complementary oligonucleotide strand, forms a complex that mimics the specific interactions between the GCN4 protein and DNA. The covalent bond connecting the oligonucleotide and peptide constitutes a part of substituted triazole, which forms due to the click reaction between the short peptide corresponding to the specific amino acid sequence of GCN4 protein (yeast transcription factor) and a DNA fragment that is recognized by the protein. DNAse footprinting demonstrated that the part of the DNA fragment that specifically interacts with the peptide in the complex is protected from DNAse activity. Moreover, the thermodynamic characteristics obtained using differential scanning calorimetry (DSC) are consistent with the interaction energies calculated at the level of metadynamics. Thus, we present an efficient approach to generate a well-defined DNA-peptide conjugate that mimics a real DNA-peptide complex. These complexes can be used to investigate DNA damage under conditions very similar to those present in the cell. Full article
(This article belongs to the Special Issue Photoactive Biological Molecules)
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