
About
Sarah Delaney is the Vernon K. Krieble Professor of Chemistry and serves as the Chair of the Department of Chemistry at Brown University. Her research focuses on nucleic acids chemistry and biology, particularly understanding the biological consequences of DNA damage. Using biochemistry, biophysics, and molecular biology methods, she probes the effects of DNA damage from the molecular to the cellular level. Her work involves synthesizing modified DNA nucleobases and studying their properties within well-defined systems, with a special interest in how DNA packaging into chromatin influences DNA repair processes. Dr. Delaney's educational background includes a B.A. in Chemistry from Middlebury College, a Ph.D. in Chemistry from Caltech, and a postdoctoral fellowship in Biological Engineering at MIT. Her research aims to elucidate the mechanisms of DNA repair and the impact of DNA damage on biological systems, contributing to a deeper understanding of DNA repair pathways and the role of chromatin structure in these processes.
Research topics
- Political Science
- Medicine
- Risk analysis (engineering)
- Chemistry
- Environmental health
- Internal medicine
- Pharmacology
- Statistics
- Nursing
- Emergency medicine
- Psychiatry
- Law
- Mathematics
- Business
Selected publications
Archives of Toxicology · 2026-05-20
articleOpen accessAbstract Designer benzodiazepines (DBZDs) are a class of new psychoactive substances (NPS) designed as legal alternatives to prescription BZDs. Bromazolam has been the most prevalent DBZD detected on the recreational market around the world; however, a new DBZD, ethylbromazolam (8-bromo-1-ethyl-6-phenyl-4 H-[1,2,4]triazolo[4,3-a][1,4]benzodiazepine; also known as bromoethylazolam) has recently emerged. In this study, the emergence of ethylbromazolam in Canada, the UK, and Australia is reported based on analysis of samples from drug checking services and in Germany based on analysis of samples seized by customs and mail services. Since November 2024, ethylbromazolam has been increasingly detected with a concurrent decrease in bromazolam detections, suggesting that its emergence is likely in response to the international control of bromazolam on 3rd December 2024. Additionally, increased detections of other DBZDs, including desalkylgidazepam (bromonordiazepam) and clobromazolam (phenazolam) have been recently observed. The in vitro α 1 β 2 γ 2 GABA A receptor activity of ethylbromazolam was determined using an automated patch clamp assay. Ethylbromazolam was found to have similar in vitro GABA A receptor activity as bromazolam (EC 50 of 10.1 nM and 15.2 nM, respectively), indicating comparable pharmacological activity and potential for harm. The market should continue to be monitored closely as it continues to evolve in response to the control of bromazolam.
Caught in the Gap: A Case of Unexpected Lactate Elevation
The Journal of Applied Laboratory Medicine · 2025-11-18
articleOpen accessSenior authorInitiation of base excision repair is modulated by nucleosome occupancy modifying sequences
DNA repair · 2025-05-23
articleSenior authorCorrespondingBiochemistry · 2025-04-14 · 2 citations
articleSenior authorCorrespondingThymine DNA glycosylase (TDG) is a DNA glycosylase involved in base excision repair (BER) with a specialized role in the regulation of transcription through the maintenance of 5′-CpG-3′ sites via active demethylation. In this work, we investigate the ability of TDG to excise modified nucleobases from the simplest unit of compacted DNA, the nucleosome core particle (NCP). We measure TDG activity on a population of NCPs with uracil (U) at various geometric positions and report that kobs for U excision from the NCP depends on positioning and dinucleotide sequence context. Specifically, TDG prefers solution accessible 5′-UpG-3′ and 5′-UpA-3′ sites. By coupling our findings with previous studies, we suggest that TDG’s stringent substrate preferences facilitate its epigenetic role through the extensive contacts made with its DNA substrate.
Structure, dynamics, and processing of 8oxoG:A in the nucleosome
bioRxiv (Cold Spring Harbor Laboratory) · 2025-09-05
preprintOpen accessEukaryotic genomic DNA is packaged into chromatin through a repeating unit known as the nucleosome. In this chromatin environment, DNA is constantly exposed to several sources of DNA damage, such as reactive oxygen species (ROS), which can lead to the formation of 8-oxo-7,8-dihydroguanine (8oxoG). 8oxoG can base pair with cytosine (8oxoG:C) or form a mutagenic base pair with adenine (8oxoG:A), which can lead to single base transversions if left unrepaired. To date, the structure and dynamics of these two possible 8oxoG base pairs in the nucleosome remain unclear. Furthermore, whether MutY homologue (MUTYH) excises 8oxoG:A base pairs in the nucleosome remains elusive. Here using a combination of cryogenic-electron microscopy, molecular dynamics simulations, and biochemistry we determined the structure and dynamics of 8oxoG:C and 8oxoG:A base pairs in the nucleosome and characterize MUTYH activity in nucleosomal DNA. We found that nucleosomal 8oxoG:C forms a stable base pair using its anti conformation, while nucleosomal 8oxoG:A forms a more dynamic base pair using its syn conformation that is unable to be processed by MUTYH. This work provides fundamental insight into the accommodation of oxidative damage in the nucleosome and how this damage contributes to increased mutagenic transversions in nucleosomal compared to linker DNA.
Clinical Biochemistry · 2025-05-21 · 2 citations
articleCommentary on Supratherapeutic Carbamazepine Concentration Following a Recent SARS-CoV-2 Infection
Clinical Chemistry · 2025-03-29
article1st authorCorrespondingClinical Biochemistry · 2024-08-23 · 13 citations
reviewSenior authorCorrespondingClinical Chemistry · 2024-10-01 · 1 citations
articleAbstract Background Point-of-care (POC) urine drug testing is a useful adjunct to self-reporting in rapid access addiction medicine settings to immediately guide patient management. However, available POC immunoassays have limitations including cross-reactivity with unrelated compounds or low sensitivity that may cause false results. Here, we assessed the performance of a multi-drug test panel by comparing against gold-standard liquid chromatography tandem mass spectrometry (LC-MS/MS) testing. Methods 102 residual urine specimens were assayed using a competitive lateral flow immunoassay (LFA) for 10 drugs: 2-ethylene-1,5-dimethyl-3,3-diphenylpyrrolidine (EDDP, methadone metabolite), buprenorphine, morphine, hydromorphone, oxycodone, fentanyl, cocaine, methamphetamine, amphetamine, and benzodiazepines (BTNX Rapid ResponseTM Multi-Drug Panel). Results were compared to those obtained by LC-MS/MS (n=67, 66%) or kinetic interaction of microparticles in solution automated immunoassay (KIMS) (Roche Diagnostics, n=35, 33%). Broad spectrum LC-MS/MS results were reviewed in entirety for discordant cases, particularly in false positives to identify the presence of any known cross-reacting compounds. Results Of 10 drugs evaluated, four demonstrated ≥95% agreement with LC-MS/MS or KIMS immunoassay (EDDP, buprenorphine, oxycodone, methamphetamine). Fentanyl demonstrated the highest false negative rate of 44% (LFA cut-off: 10 ng/mL) followed by amphetamines (22%, cut-off: 1000 ng/mL). Morphine and hydromorphone demonstrated false positive rates of 14% and 18%, respectively, with most cases likely due to cross-reacting opiate or opioid metabolites. Benzodiazepines (target: Oxazepam) demonstrated false positive and negative rates of 13% and 24%, respectively. Conclusions To our knowledge, this is the first study to evaluate the performance of the BTNX multi-drug test panel against definitive testing in urine samples. While good concordance was observed for most drugs, high rates of discordant results for fentanyl and others emphasize the need for confirmatory testing by methods with higher sensitivity and specificity. Careful consideration prior to implementation would be essential, including physician education, interpretative comments, and training resources.
Global screening of base excision repair in nucleosome core particles
DNA repair · 2024-10-19 · 10 citations
articleOpen accessSenior authorCorresponding
Recent grants
NIH · $27.6M · 2014
Modulation of DNA Repair by the Protein Component of Chromatin
NSF · $860k · 2018–2023
Inflammation as a Mediator of Dynamic DNA Mutations
NIH · $2.2M · 2010–2016
NIH · $2.0M · 2023–2028
NIH resubmission Deyu Li - Etheno adductome and repair pathways
NIH · $1.6M · 2023–2027
Frequent coauthors
- 27 shared
Daniel R. Beriault
- 21 shared
Catherine B. Volle
Cornell University
- 20 shared
Chuxuan Li
Rice University
- 20 shared
Daniel A. Jarem
Materials Systems (United States)
- 16 shared
Paul J. Caffrey
New England Biolabs (United States)
- 16 shared
Katelyn L. Rioux
Brown University
- 15 shared
David Colantonio
Ottawa Hospital
- 14 shared
Craig J. Yennie
Providence College
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