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Artikel ; Online: Interactive computational and experimental approaches improve the sensitivity of periplasmic binding protein-based nicotine biosensors for measurements in biofluids.

Haloi, Nandan / Huang, Shan / Nichols, Aaron L / Fine, Eve J / Friesenhahn, Nicholas J / Marotta, Christopher B / Dougherty, Dennis A / Lindahl, Erik / Howard, Rebecca J / Mayo, Stephen L / Lester, Henry A

Protein engineering, design & selection : PEDS

2024 Band 37

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 ... ...

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 binding protein (PBP) domain appears tilted in iNicSnFR12 relative to iNicSnFR3a, likely altering allosteric network(s) that link the ligand binding site to the fluorophore. In thermal melt experiments, nicotine stabilized the PBP of the tested iNicSnFR variants. iNicSnFR12 resolved nicotine in diluted mouse and human serum at 100 nM, the peak [nicotine] that occurs during smoking or vaping, and possibly at the decreasing levels during intervals between sessions. NicSnFR12 was also partially activated by unidentified endogenous ligand(s) in biofluids. Improved iNicSnFR12 variants could become the molecular sensors in continuous nicotine monitors for animal and human biofluids.
Mesh-Begriff(e)	Humans ; Animals ; Mice ; Nicotine ; Periplasmic Binding Proteins/chemistry ; Periplasmic Binding Proteins/metabolism ; Ligands ; Binding Sites ; Biosensing Techniques
Chemische Substanzen	Nicotine (6M3C89ZY6R) ; Periplasmic Binding Proteins ; Ligands
Sprache	Englisch
Erscheinungsdatum	2024-01-30
Erscheinungsland	England
Dokumenttyp	Journal Article
ZDB-ID	1466729-0
ISSN	1741-0134 ; 1741-0126
ISSN (online)	1741-0134
ISSN	1741-0126
DOI	10.1093/protein/gzae003
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: Interactive computational and experimental approaches improve the sensitivity of periplasmic binding protein-based nicotine biosensors for measurements in biofluids.

bioRxiv : the preprint server for biology

2024

Abstract: We developed fluorescent protein sensors for nicotine with improved sensitivity. For iNicSnFR12 at pH 7.4, the proportionality constant ... ...

Abstract	We developed fluorescent protein sensors for nicotine with improved sensitivity. For iNicSnFR12 at pH 7.4, the proportionality constant for
Sprache	Englisch
Erscheinungsdatum	2024-01-18
Erscheinungsland	United States
Dokumenttyp	Preprint
DOI	10.1101/2023.01.16.524298
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Selective Serotonin Reuptake Inhibitors within Cells: Temporal Resolution in Cytoplasm, Endoplasmic Reticulum, and Membrane.

Nichols, Aaron L / Blumenfeld, Zack / Luebbert, Laura / Knox, Hailey J / Muthusamy, Anand K / Marvin, Jonathan S / Kim, Charlene H / Grant, Stephen N / Walton, David P / Cohen, Bruce N / Hammar, Rebekkah / Looger, Loren / Artursson, Per / Dougherty, Dennis A / Lester, Henry A

The Journal of neuroscience : the official journal of the Society for Neuroscience

2023 Band 43, Heft 13, Seite(n) 2222–2241

Abstract: Selective serotonin reuptake inhibitors (SSRIs) are the most prescribed treatment for individuals experiencing major depressive disorder. The therapeutic mechanisms that take place before, during, or after SSRIs bind the serotonin transporter (SERT) are ... ...

Abstract	Selective serotonin reuptake inhibitors (SSRIs) are the most prescribed treatment for individuals experiencing major depressive disorder. The therapeutic mechanisms that take place before, during, or after SSRIs bind the serotonin transporter (SERT) are poorly understood, partially because no studies exist on the cellular and subcellular pharmacokinetic properties of SSRIs in living cells. We studied escitalopram and fluoxetine using new intensity-based, drug-sensing fluorescent reporters targeted to the plasma membrane, cytoplasm, or endoplasmic reticulum (ER) of cultured neurons and mammalian cell lines. We also used chemical detection of drug within cells and phospholipid membranes. The drugs attain equilibrium in neuronal cytoplasm and ER at approximately the same concentration as the externally applied solution, with time constants of a few s (escitalopram) or 200-300 s (fluoxetine). Simultaneously, the drugs accumulate within lipid membranes by ≥18-fold (escitalopram) or 180-fold (fluoxetine), and possibly by much larger factors. Both drugs leave cytoplasm, lumen, and membranes just as quickly during washout. We synthesized membrane-impermeant quaternary amine derivatives of the two SSRIs. The quaternary derivatives are substantially excluded from membrane, cytoplasm, and ER for >2.4 h. They inhibit SERT transport-associated currents sixfold or 11-fold less potently than the SSRIs (escitalopram or fluoxetine derivative, respectively), providing useful probes for distinguishing compartmentalized SSRI effects. Although our measurements are orders of magnitude faster than the therapeutic lag of SSRIs, these data suggest that SSRI-SERT interactions within organelles or membranes may play roles during either the therapeutic effects or the antidepressant discontinuation syndrome.
Mesh-Begriff(e)	Animals ; Humans ; Selective Serotonin Reuptake Inhibitors/pharmacology ; Fluoxetine/pharmacology ; Depressive Disorder, Major ; Escitalopram ; Serotonin/metabolism ; Serotonin Plasma Membrane Transport Proteins/metabolism ; Endoplasmic Reticulum/metabolism ; Citalopram/pharmacology ; Mammals
Chemische Substanzen	Selective Serotonin Reuptake Inhibitors ; Fluoxetine (01K63SUP8D) ; Escitalopram (4O4S742ANY) ; Serotonin (333DO1RDJY) ; Serotonin Plasma Membrane Transport Proteins ; Citalopram (0DHU5B8D6V)
Sprache	Englisch
Erscheinungsdatum	2023-03-03
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	604637-x
ISSN	1529-2401 ; 0270-6474
ISSN (online)	1529-2401
ISSN	0270-6474
DOI	10.1523/JNEUROSCI.1519-22.2022
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Fluorescence Screens for Identifying Central Nervous System-Acting Drug-Biosensor Pairs for Subcellular and Supracellular Pharmacokinetics.

Beatty, Zoe G / Muthusamy, Anand K / Unger, Elizabeth K / Dougherty, Dennis A / Tian, Lin / Looger, Loren L / Shivange, Amol V / Bera, Kallol / Lester, Henry A / Nichols, Aaron L

Bio-protocol

2022 Band 12, Heft 22

Abstract: Subcellular pharmacokinetic measurements have informed the study of central nervous system (CNS)-acting drug mechanisms. Recent investigations have been enhanced by the use of genetically encoded fluorescent biosensors for drugs of interest at the plasma ...

Abstract	Subcellular pharmacokinetic measurements have informed the study of central nervous system (CNS)-acting drug mechanisms. Recent investigations have been enhanced by the use of genetically encoded fluorescent biosensors for drugs of interest at the plasma membrane and in organelles. We describe screening and validation protocols for identifying hit pairs comprising a drug and biosensor, with each screen including 13-18 candidate biosensors and 44-84 candidate drugs. After a favorable hit pair is identified and validated via these protocols, the biosensor is then optimized, as described in other papers, for sensitivity and selectivity to the drug. We also show sample hit pair data that may lead to future intensity-based drug-sensing fluorescent reporters (iDrugSnFRs). These protocols will assist scientists to use fluorescence responses as criteria in identifying favorable fluorescent biosensor variants for CNS-acting drugs that presently have no corresponding biosensor partner.
Sprache	Englisch
Erscheinungsdatum	2022-11-20
Erscheinungsland	United States
Dokumenttyp	Journal Article
ZDB-ID	2833269-6
ISSN	2331-8325 ; 2331-8325
ISSN (online)	2331-8325
ISSN	2331-8325
DOI	10.21769/BioProtoc.4551
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Three Mutations Convert the Selectivity of a Protein Sensor from Nicotinic Agonists to S-Methadone for Use in Cells, Organelles, and Biofluids.

Muthusamy, Anand K / Kim, Charlene H / Virgil, Scott C / Knox, Hailey J / Marvin, Jonathan S / Nichols, Aaron L / Cohen, Bruce N / Dougherty, Dennis A / Looger, Loren L / Lester, Henry A

Journal of the American Chemical Society

2022 Band 144, Heft 19, Seite(n) 8480–8486

Abstract: We report a reagentless, intensity-based S-methadone fluorescent sensor, iS-methadoneSnFR, consisting of a circularly permuted GFP inserted within the sequence of a mutated bacterial periplasmic binding protein (PBP). We evolved a previously reported ... ...

Abstract	We report a reagentless, intensity-based S-methadone fluorescent sensor, iS-methadoneSnFR, consisting of a circularly permuted GFP inserted within the sequence of a mutated bacterial periplasmic binding protein (PBP). We evolved a previously reported nicotine-binding PBP to become a selective S-methadone-binding sensor, via three mutations in the PBP's second shell and hinge regions. iS-methadoneSnFR displays the necessary sensitivity, kinetics, and selectivity─notably enantioselectivity against R-methadone─for biological applications. Robust iS-methadoneSnFR responses in human sweat and saliva and mouse serum enable diagnostic uses. Expression and imaging in mammalian cells demonstrate that S-methadone enters at least two organelles and undergoes acid trapping in the Golgi apparatus, where opioid receptors can signal. This work shows a straightforward strategy in adapting existing PBPs to serve real-time applications ranging from subcellular to personal pharmacokinetics.
Mesh-Begriff(e)	Animals ; Mammals/metabolism ; Methadone ; Mice ; Mutation ; Nicotinic Agonists ; Organelles/metabolism ; Periplasmic Binding Proteins
Chemische Substanzen	Nicotinic Agonists ; Periplasmic Binding Proteins ; Methadone (UC6VBE7V1Z)
Sprache	Englisch
Erscheinungsdatum	2022-04-21
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.2c02323
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Buch ; Artikel ; Online: Successful Cessation Programs that Reduce Comorbidity May Explain Surprisingly Low Smoking Rates Among Hospitalized COVID-19 Patients

Cohen, Bruce N. / Nichols, Aaron L. / Grant, Stephen / Blumenfeld, Zach / Dougherty, Dennis A. / Alvarez, R. Michael / Ritz, Beate / Lester, Henry A.

2020

Abstract: A recent, non-peer-reviewed meta-analysis suggests that smoking may reduce the risk of hospitalization with COVID-19 because the prevalence of smoking among hospitalized COVID-19 is less than that of the general population. However, there are alternative ...

Abstract	A recent, non-peer-reviewed meta-analysis suggests that smoking may reduce the risk of hospitalization with COVID-19 because the prevalence of smoking among hospitalized COVID-19 is less than that of the general population. However, there are alternative explanations for this phenomena based on (1) the failure to report, or accurately record, smoking history during emergency hospital admissions and (2) a pre-disposition to avoid smoking among COVID-19 patients with tobacco-related comorbidities (a type of “reverse” causation). For example, urine testing of hospitalized patients in Australia for cotinine showed that smokers were under-counted by 37% because incoming patients failed to inform staff about their smoking behavior. Face-to-face interviews can introduce bias into the responses to attitudinal and behavioral questions not present in the self-completion interviews typically used to measure smoking prevalence in the general population. Subjects in face-to-face interviews may be unwilling to admit socially undesirable behavior and attitudes under direct questioning. Reverse causation may also contribute to the difference between smoking prevalence in the COVID-19 and general population. Patients hospitalized with COVID-19 may be simply less prone to use tobacco than the general population. A potentially robust “reverse causation” hypothesis for reduced prevalence of smokers in the COVID-19 population is the enrichment of patients in that population with serious comorbidities that motivates them to quit smoking. We judge that this “smoking cessation” mechanism may account for a significant fraction of the reduced prevalence of smokers in the COVID-19 population. Testing this hypothesis will require a focused research program.
Schlagwörter	covid19
Thema/Rubrik (Code)	610
Erscheinungsdatum	2020-05-26
Erscheinungsland	us
Dokumenttyp	Buch ; Artikel ; Online
Datenquelle	BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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Artikel ; Online: Fluorescence activation mechanism and imaging of drug permeation with new sensors for smoking-cessation ligands.

Nichols, Aaron L / Blumenfeld, Zack / Fan, Chengcheng / Luebbert, Laura / Blom, Annet E M / Cohen, Bruce N / Marvin, Jonathan S / Borden, Philip M / Kim, Charlene H / Muthusamy, Anand K / Shivange, Amol V / Knox, Hailey J / Campello, Hugo Rego / Wang, Jonathan H / Dougherty, Dennis A / Looger, Loren L / Gallagher, Timothy / Rees, Douglas C / Lester, Henry A

eLife

2022 Band 11

Abstract: Nicotinic partial agonists provide an accepted aid for smoking cessation and thus contribute to decreasing tobacco-related disease. Improved drugs constitute a continued area of study. However, there remains no reductionist method to examine the cellular ...

Abstract	Nicotinic partial agonists provide an accepted aid for smoking cessation and thus contribute to decreasing tobacco-related disease. Improved drugs constitute a continued area of study. However, there remains no reductionist method to examine the cellular and subcellular pharmacokinetic properties of these compounds in living cells. Here, we developed new intensity-based drug-sensing fluorescent reporters (iDrugSnFRs) for the nicotinic partial agonists dianicline, cytisine, and two cytisine derivatives - 10-fluorocytisine and 9-bromo-10-ethylcytisine. We report the first atomic-scale structures of liganded periplasmic binding protein-based biosensors, accelerating development of iDrugSnFRs and also explaining the activation mechanism. The nicotinic iDrugSnFRs detect their drug partners in solution, as well as at the plasma membrane (PM) and in the endoplasmic reticulum (ER) of cell lines and mouse hippocampal neurons. At the PM, the speed of solution changes limits the growth and decay rates of the fluorescence response in almost all cases. In contrast, we found that rates of membrane crossing differ among these nicotinic drugs by >30-fold. The new nicotinic iDrugSnFRs provide insight into the real-time pharmacokinetic properties of nicotinic agonists and provide a methodology whereby iDrugSnFRs can inform both pharmaceutical neuroscience and addiction neuroscience.
Mesh-Begriff(e)	Alkaloids/chemistry ; Alkaloids/metabolism ; Animals ; Azepines/chemistry ; Azocines/chemistry ; Azocines/metabolism ; Fluorescence ; Heterocyclic Compounds, 4 or More Rings/chemistry ; Humans ; Ligands ; Mice ; Nicotinic Agonists/chemistry ; Quinolizines/chemistry ; Quinolizines/metabolism ; Smoking Cessation
Chemische Substanzen	Alkaloids ; Azepines ; Azocines ; Heterocyclic Compounds, 4 or More Rings ; Ligands ; Nicotinic Agonists ; Quinolizines ; cytisine (53S5U404NU) ; dianicline (Y0SNM34C6O)
Sprache	Englisch
Erscheinungsdatum	2022-01-04
Erscheinungsland	England
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.74648
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Correction: Fluorescence activation mechanism and imaging of drug permeation with new sensors for smoking-cessation ligands.

eLife

2022 Band 11

Sprache	Englisch
Erscheinungsdatum	2022-12-15
Erscheinungsland	England
Dokumenttyp	Published Erratum
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.85479
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: α1-FANGs: Protein Ligands Selective for the α-Bungarotoxin Site of the α1-Nicotinic Acetylcholine Receptor.

Nichols, Aaron L / Noridomi, Kaori / Hughes, Christopher R / Jalali-Yazdi, Farzad / Eaton, J Brek / Lai, Lan Huong / Advani, Gaurav / Lukas, Ronald J / Lester, Henry A / Chen, Lin / Roberts, Richard W

ACS chemical biology

2018 Band 13, Heft 9, Seite(n) 2568–2576

Abstract: Nicotinic acetylcholine receptors (nAChRs) are pentameric ligand-gated ion channels that play a central role in neuronal and neuromuscular signal transduction. Here, we have developed FANG ligands, fibronectin antibody-mimetic nicotinic acetylcholine ... ...

Abstract	Nicotinic acetylcholine receptors (nAChRs) are pentameric ligand-gated ion channels that play a central role in neuronal and neuromuscular signal transduction. Here, we have developed FANG ligands, fibronectin antibody-mimetic nicotinic acetylcholine receptor-generated ligands, using mRNA display. We generated a 1 trillion-member primary e10FnIII library to target a stabilized α1 nicotinic subunit (α211). This library yielded 270000 independent potential protein binding ligands. The lead sequence, α1-FANG1, represented 25% of all library sequences, showed the highest-affinity binding, and competed with α-bungarotoxin (α-Btx). To improve this clone, a new library based on α1-FANG1 was subjected to heat, protease, binding, off-rate selective pressures, and point mutations. This resulted in α1-FANG2 and α1-FANG3. These proteins bind α211 with K
Mesh-Begriff(e)	Animals ; Bungarotoxins/metabolism ; Fibronectins/genetics ; Fibronectins/metabolism ; Gene Library ; Humans ; Ligands ; Mice ; Point Mutation ; Protein Binding ; Protein Subunits/metabolism ; Receptors, Nicotinic/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Thermodynamics ; Xenopus
Chemische Substanzen	Bungarotoxins ; Fibronectins ; Ligands ; Protein Subunits ; Receptors, Nicotinic ; Recombinant Proteins
Schlagwörter	covid19
Sprache	Englisch
Erscheinungsdatum	2018-08-13
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1554-8937
ISSN (online)	1554-8937
DOI	10.1021/acschembio.8b00513
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: Biosensors Show the Pharmacokinetics of S-Ketamine in the Endoplasmic Reticulum.

Bera, Kallol / Kamajaya, Aron / Shivange, Amol V / Muthusamy, Anand K / Nichols, Aaron L / Borden, Philip M / Grant, Stephen / Jeon, Janice / Lin, Elaine / Bishara, Ishak / Chin, Theodore M / Cohen, Bruce N / Kim, Charlene H / Unger, Elizabeth K / Tian, Lin / Marvin, Jonathan S / Looger, Loren L / Lester, Henry A

Frontiers in cellular neuroscience

2019 Band 13, Seite(n) 499

Abstract: The target for the "rapid" (<24 h) antidepressant effects of S-ketamine is unknown, vitiating programs to rationally develop more effective rapid antidepressants. To describe a drug's target, one must first understand the compartments entered by the drug, ...

Abstract	The target for the "rapid" (<24 h) antidepressant effects of S-ketamine is unknown, vitiating programs to rationally develop more effective rapid antidepressants. To describe a drug's target, one must first understand the compartments entered by the drug, at all levels-the organ, the cell, and the organelle. We have, therefore, developed molecular tools to measure the subcellular, organellar pharmacokinetics of S-ketamine. The tools are genetically encoded intensity-based S-ketamine-sensing fluorescent reporters, iSKetSnFR1 and iSKetSnFR2. In solution, these biosensors respond to S-ketamine with a sensitivity, S-slope = delta(F/F
Sprache	Englisch
Erscheinungsdatum	2019-11-12
Erscheinungsland	Switzerland
Dokumenttyp	Journal Article
ZDB-ID	2452963-1
ISSN	1662-5102
ISSN	1662-5102
DOI	10.3389/fncel.2019.00499
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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