{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Haloi N"],"funding":["California Tobacco-Related Disease Research Program","Swedish National Infrastructure for Computing","Marie Sklodowska-Curie Postdoctoral Fellowship","NIDA NIH HHS","Swedish e-Science Research Centre (SeRC), and the BioExcel Center of Excellence","California TRDRP","Knut and Alice Wallenberg Foundation, the Swedish Research Council","National Institute on Drug Abuse","National Institute of General Medical Sciences","NIGMS NIH HHS","Karolina through EuroHPC"],"pagination":["gzae003"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10896302"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["37"],"pubmed_abstract":["We developed fluorescent protein sensors for nicotine with improved sensitivity. For iNicSnFR12 at pH 7.4, the proportionality constant for ∆F/F0vs [nicotine] (δ-slope, 2.7 μM-1) is 6.1-fold higher than the previously reported iNicSnFR3a. The activated state of iNicSnFR12 has a fluorescence quantum yield of at least 0.6. We measured similar dose-response relations for the nicotine-induced absorbance increase and fluorescence increase, suggesting that the absorbance increase leads to the fluorescence increase via the previously described nicotine-induced conformational change, the 'candle snuffer' mechanism. Molecular dynamics (MD) simulations identified a binding pose for nicotine, previously indeterminate from experimental data. MD simulations also showed that Helix 4 of the periplasmic b"],"journal":["Protein engineering, design & selection : PEDS"],"pubmed_title":["Interactive computational and experimental approaches improve the sensitivity of periplasmic binding protein-based nicotine biosensors for measurements in biofluids."],"pmcid":["PMC10896302"],"funding_grant_id":["27FT-0022","2019-02433","GM-123582","2021-05806","SNIC2022/3-40","EHPC-REG-2021R0074","EU-823830","DA049140","101107036","T29IR0455","R21 DA049140","27IP-0057","R01 GM123582"],"pubmed_authors":["Lindahl E","Huang S","Howard RJ","Dougherty DA","Fine EJ","Haloi N","Friesenhahn NJ","Lester HA","Nichols AL","Mayo SL","Marotta CB"],"additional_accession":[]},"is_claimable":false,"name":"Interactive computational and experimental approaches improve the sensitivity of periplasmic binding protein-based nicotine biosensors for measurements in biofluids.","description":"We developed fluorescent protein sensors for nicotine with improved sensitivity. For iNicSnFR12 at pH 7.4, the proportionality constant for ∆F/F0vs [nicotine] (δ-slope, 2.7 μM-1) is 6.1-fold higher than the previously reported iNicSnFR3a. The activated state of iNicSnFR12 has a fluorescence quantum yield of at least 0.6. We measured similar dose-response relations for the nicotine-induced absorbance increase and fluorescence increase, suggesting that the absorbance increase leads to the fluorescence increase via the previously described nicotine-induced conformational change, the 'candle snuffer' mechanism. Molecular dynamics (MD) simulations identified a binding pose for nicotine, previously indeterminate from experimental data. MD simulations also showed that Helix 4 of the periplasmic b","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jan","modification":"2026-06-02T11:58:35.882Z","creation":"2025-04-03T23:23:39.743Z"},"accession":"S-EPMC10896302","cross_references":{"pubmed":["38302088"],"doi":["10.1093/protein/gzae003"]}}