Development and validation of a high-throughput method for the quantitative analysis of d-amphetamine in rat blood using liquid chromatography/MS3 on a hybrid triple quadrupole-linear ion trap mass spectrometer and its application to a pharmacokinetic study

Cesari, Nicola Semprini; Fontana, Stefano; Montanari, Dino; Braggio, Simone

doi:10.1016/j.jchromb.2009.11.009

Cited by 21 publications

(9 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As the half-life of i.p. d-amphetamine is approximately 1 h in rats compared to 6–7 h in children with ADHD [68–70], treatments were administered 30 min prior to behavioral testing in the strategy set shifting task. This allowed peak monoamine responses to occur and ensured that plasma levels reached clinical significance during behavioral testing.…”

Section: Methodsmentioning

confidence: 99%

Adolescent d-amphetamine treatment in a rodent model of ADHD: Pro-cognitive effects in adolescence without an impact on cocaine cue reactivity in adulthood

Jordan

Taylor

Dwoskin

et al. 2016

Behavioural Brain Research

View full text Add to dashboard Cite

Attention-deficit/hyperactivity disorder (ADHD) is comorbid with cocaine abuse. Whereas initiating ADHD medication in childhood does not alter later cocaine abuse risk, initiating medication during adolescence may increase risk. Preclinical work in the Spontaneously Hypertensive Rat (SHR) model of ADHD found that adolescent methylphenidate increased cocaine self-administration in adulthood, suggesting a need to identify alternatively efficacious medications for teens with ADHD. We examined effects of adolescent d-amphetamine treatment on strategy set shifting performance during adolescence and on cocaine self-administration and reinstatement of cocaine-seeking behavior (cue reactivity) during adulthood in male SHR, Wistar-Kyoto (inbred control), and Wistar (outbred control) rats. During the set shift phase, adolescent SHR needed more trials and had a longer latency to reach criterion, made more regressive errors and trial omissions, and exhibited slower and more variable lever press reaction times. d-Amphetamine improved performance only in SHR by increasing choice accuracy and decreasing errors and latency to criterion. In adulthood, SHR self-administered more cocaine, made more cocaine-seeking responses, and took longer to extinguish lever responding than control strains. Adolescent d-amphetamine did not alter cocaine self-administration in adult rats of any strain, but reduced cocaine seeking during the first of seven reinstatement test sessions in adult SHR. These findings highlight utility of SHR in modeling cognitive dysfunction and comorbid cocaine abuse in ADHD. Unlike methylphenidate, d-amphetamine improved several aspects of flexible learning in adolescent SHR and did not increase cocaine intake or cue reactivity in adult SHR. Thus, adolescent d-amphetamine was superior to methylphenidate in this ADHD model.

show abstract

Section: Methodsmentioning

confidence: 99%

Adolescent d-amphetamine treatment in a rodent model of ADHD: Pro-cognitive effects in adolescence without an impact on cocaine cue reactivity in adulthood

Jordan

Taylor

Dwoskin

et al. 2016

Behavioural Brain Research

View full text Add to dashboard Cite

show abstract

“…Considering the complexity of the analysed matrices, highly selective methods are required to allow rapid analysis of AA at low concentrations (ng g −1 ). The use of MS operated in multistage fragmentation mode (MS 3 ) provides outstanding selectivity in quantitative applications aimed at the analysis of various small molecules of interest in complex samples, such as drugs in biological fluids or pesticides and mycotoxins in cereals (Cesari et al 2010;Lim et al 2012;Li et al 2013). The monitoring of MS 3 fragmentation patterns may enable the elimination of co-eluting interferences and background noise, thus increasing the signal-to-noise ratio (S/N) for some analytes.…”

Section: Introductionmentioning

confidence: 99%

Quantification of aristolochic acids I and II in herbal dietary supplements by ultra-high-performance liquid chromatography–multistage fragmentation mass spectrometry

Václavík¹,

Krynitsky²,

Rader³

2014

Food Additives & Contaminants: Part A

View full text Add to dashboard Cite

A rapid, selective and sensitive ultra-high-performance liquid chromatography-multistage fragmentation mass spectrometry (UHPLC-MS³) method was developed and evaluated for the determination of aristolochic acids I and II (AA I and II) in herbal dietary supplements. A hybrid triple quadrupole/linear ion-trap mass spectrometry was used to monitor MS³ ion transitions m/z 359.2 > 298.1 > 268.0 and m/z 329.2 > 268.2 > 238.0 to detect AA I and II, respectively. The extraction and clean-up of target analytes from dry powdered samples was performed using the quick, easy, cheap, effective, rugged and safe (QuEChERS) procedure. Herbal liquid extracts were analysed directly. Average recoveries ranged from 89% to 112%, with relative standard deviations (RSDs) ranging from 3% to 16%. Limits of quantification (LOQs) estimated for three selected matrices were as follows (AA I/II): 5/10 ng g⁻¹ (tablets); 25/50 ng g⁻¹ (capsules); and 2.5/5.0 ng ml⁻¹ (liquid herbal extract). The method was applied in a limited survey of 30 herbal products marketed in the United States via the Internet. AA I and II were detected in 20% and 7%, respectively, of tested samples.

show abstract

“…MS 3 technology was recently implemented on a hydrid quadrupole-linear ion trap mass spectrometer for the quantification of drug molecules in biological fluids. Detection limits were improved significantly in the presence of interference [18]. Similarly, peptide specificity is improved by this additional fragmentation event, and background noise can be significantly reduced.…”

Section: Methodsmentioning

confidence: 99%

Constrained selected reaction monitoring: Quantification of selected post-translational modifications and protein isoforms

Liu

Jin

O’Brien

et al. 2013

Methods

View full text Add to dashboard Cite

Selected reaction monitoring (SRM) is a mass spectrometry method that can target signature peptides to provide for the detection and quantitation of specific proteins in complex biological samples. When quantifying a protein, peptides are generated using a specific protease such as trypsin, allowing the choice of signature peptides with robust signals. In contrast, signature peptide selection can be constrained when the goal is to monitor a specific post-translational modification (PTM) or protein isoform as the signature peptide must include the amino acid residue(s) of PTM attachment or sequence variation. This can force the selection of a signature peptide with a weak SRM response or one that is confounded by high background. In this article, additional steps that can be optimized to maximize peptide selection and assay performance of constrained SRM assays are discussed including tuning instrument parameters, fragmenting product ions, using a different protease, and enriching the sample. Examples are provided for selection of phosphorylated or citrullinated peptides and protein isoforms.

show abstract

Development and validation of a high-throughput method for the quantitative analysis of d-amphetamine in rat blood using liquid chromatography/MS3 on a hybrid triple quadrupole-linear ion trap mass spectrometer and its application to a pharmacokinetic study

Cited by 21 publications

References 18 publications

Adolescent d-amphetamine treatment in a rodent model of ADHD: Pro-cognitive effects in adolescence without an impact on cocaine cue reactivity in adulthood

Adolescent d-amphetamine treatment in a rodent model of ADHD: Pro-cognitive effects in adolescence without an impact on cocaine cue reactivity in adulthood

Quantification of aristolochic acids I and II in herbal dietary supplements by ultra-high-performance liquid chromatography–multistage fragmentation mass spectrometry

Constrained selected reaction monitoring: Quantification of selected post-translational modifications and protein isoforms

Contact Info

Product

Resources

About