Circular Dichroism (CD), Bruker Avance DRX 400 MHz spectrometer<\/strong>: Asymmetric synthesis of an atropisomeric \u03b2-carboline via regioselective intermolecular Rh(I)-catalyzed [2 + 2 + 2] cyclotrimerization. Tetrahedron Letters 2024, 146, p155187.<\/p>\n AB Sciex 4600 Mass Spectrometry:<\/strong> Stable Interstrand Cross-Links Generated from the Repair of 1,N6-Ethenoadenine in DNA by \u03b1-Ketoglutarate\/Fe(II)-Dependent Dioxygenase ALKBH2. Journal of American Chemical Society 2024, 146, p10381.<\/p>\n Cai, A.; LaVigne, K. L.; Crisalli, A. M.; Delaney, S.; Min, J.-H.; Cho, B. P. Comparative studies on bulky DNA damage binding by nucleotide excision repair proteins using surface plasmon resonance, differential scanning fluorometry, and DNase I footprinting. Chemical Research in Toxicology<\/strong> 2025<\/strong>, 38<\/em> (1), 206\u2013215. DOI: https:\/\/doi.org\/10.1021\/acs.chemrestox.4c00456<\/a>.<\/p>\n![\"\"](\"https:\/\/web.uri.edu\/riinbre\/wp-content\/uploads\/sites\/1497\/Picture7-1-225x300.jpg\")
This paper highlights a highly collaborative work among colleagues from three universities, providing critical insights into how the repair protein XPC recognizes and interacts with bulky DNA lesions. Led by the RI-INBRE Core Director Ang Cai under the guidance of the RI-INBRE Program Director Bongsup Cho (URI) with key contributions from Dr. Sarah Delaney and Katelyn L. LaVigne at Brown University, and Junghyun Min at Balor University, the study investigates how the human XPC protein and its yeast ortholog Rad4 interact with bulky di-FAAF-modified DNA lesions. Using advanced CRCF items\u2014surface plasmon resonance (SPR)\/Biacore T200 instrument<\/strong> and differential scanning fluorimetry (DSF)\/Tycho NT.6 system<\/strong>, as well as DNase I footprinting\u2014the team revealed that XPC binds damaged DNA with 10-fold greater affinity and 16-fold stronger retention than Rad4, while Rad4 undergoes more significant conformational changes upon binding. DNase I footprinting identified a 7-nucleotide protected region on the complementary strand, showing Rad4\u2019s interaction with the undamaged DNA. This collaborative work, leveraging cutting-edge instrumentation from CRCF<\/strong>, provides critical insights into DNA damage recognition and repair mechanisms, with implications for cancer research and therapeutic development.<\/p>\n
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Riley R. Hughes, Circular Dichroism (CD) spectroscopy was used to analyze the enantiomers 10-entA and 10-entB at the Central Research Core Facility (CRCF), providing crucial insights into their chiral characteristics<\/p>\n![\"\"](\"https:\/\/web.uri.edu\/riinbre\/wp-content\/uploads\/sites\/1497\/Picture1-300x200.jpg\")
This paper, published in the Journal of the American Chemical Society<\/em>, discovered a new type of DNA damage that happens when cells try to fix a specific DNA problem called 1,N6N<\/em>6-ethenoadenine (eAeA<\/em>), which is caused by things like inflammation or exposure to harmful chemicals. The damage, called an interstrand cross-link (ICL), occurs when a repair enzyme called ALKBH2 accidentally creates a strong bond between the damaged DNA and a healthy part of the opposite DNA strand. This bond can block critical cell processes like copying or reading DNA, which could lead to cell death or disease. The researchers used sophisticated instrumentation <\/strong>at CRCF such as AB Sciex 4600 mass spectrometry<\/strong>, ultra centrifuges,<\/strong> and computer simulations to show how this happens and even found evidence in human cells. This discovery helps us understand how DNA repair can sometimes go wrong and cause more harm, especially in conditions like cancer or after exposure to toxins. <\/p>\n![\"\"](\"https:\/\/web.uri.edu\/riinbre\/wp-content\/uploads\/sites\/1497\/Picture2-1.jpg\")
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