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Hire Dr. Mohammed S.

United Kingdom

USD 30 /hr

Experienced Medical Researcher | Expert in Pharmacology, Scientific Communication & Strategic Marketing Initiatives

Profile Summary

A highly accomplished medical professional with over a decade of experience in academia, research, operations management, and diagnostics. Expertise in GPCR signaling, drug development, regulatory compliance, and stakeholder engagement. Proven ability to bridge the gap between scientific research and commercial strategy, supporting data-driven decision-making and market positioning.

Subject Matter Expertise

• ☆ Neuroscience
• ☆ Neuropharmacology
• ☆ Pharmacy
• ☆ Drug Development
• ☆ Small Molecule Drug Development
• ☆ Drug Substance Characterization
• ☆ Drug-Drug Interactions
• ☆ Preclinical Research
• ☆ Pharmacogenomics
• ☆ Preclinical Pharmacology
• ☆ In vitro Preclinical Toxciology
• ☆ Drug Efficacy Testing
• ☆ Gene Therapy
• ☆ Pharmaceutical Management

Services

• Writing
• Research
• Consulting
• Data & AI
• Product Development

Writing Medical Writing, Technical Writing, General Proofreading & Editing

Research Scientific and Technical Research

Consulting Business Strategy Consulting, Healthcare Consulting, Operations Consulting, Scientific and Technical Consulting

Data & AI Image Analysis

Product Development Stability/Shelf Life Testing, Product Evaluation, Material Sourcing, Product Launch Support

Work Experience

Student Mentor

Glasgow Caledonian University

October 2024 - Present

Scientific Content Editor

British Pharmacological Society

July 2024 - Present

Research Associate

Imperial College London

March 2023 - Present

Pharmacist

Ministry of Interior

2011 - Present

Operation Manager

Est-Ethics Ltd

June 2022 - April 2023

Senior Scientist/ Team Leader

Cignpost Diagnostics

January 2021 - June 2022

Postgraduate demonstrator

University of Strathclyde

January 2016 - January 2020

Education

PhD (SIPBS)

University of Strathclyde

2016 - 2021

MSc (Life science)

Glasgow Caledonian University

September 2014 - September 2015

(Pharmacy College )

King Saud University

2003 - 2010

Certifications

• Certification details not provided.

Publications

JOURNAL ARTICLE

On synthetic instrument response functions of time-correlated single-photon counting based fluorescence lifetime imaging analysis @article{2f9371be3d6240f8b4b75cea730651e5, title = "On synthetic instrument response functions of time-correlated single-photon counting based fluorescence lifetime imaging analysis", abstract = "Time-correlated single-photon counting (TCSPC) has been the gold standard for fluorescence lifetime imaging (FLIM) techniques due to its high signal-to-noize ratio and high temporal resolution. The sensor system's temporal instrument response function (IRF) should be considered in the deconvolution procedure to extract the real fluorescence decay to compensate for the distortion on measured decays contributed by the system imperfections. However, to measure the instrument response function is not trivial, and the measurement setup is different from measuring the real fluorescence. On the other hand, automatic synthetic IRFs can be directly derived from the recorded decay profiles and provide appropriate accuracy. This paper proposed and examined a synthetic IRF strategy. Compared with traditional automatic synthetic IRFs, the new proposed automatic synthetic IRF shows a broader dynamic range and better accuracy. To evaluate its performance, we examined simulated data using nonlinear least square deconvolution based on both the Levenberg-Marquardt algorithm and the Laguerre expansion method for bi-exponential fluorescence decays. Furthermore, experimental FLIM data of cells were also analyzed using the proposed synthetic IRF. The results from both the simulated data and experimental FLIM data show that the proposed synthetic IRF has a better performance compared to traditional synthetic IRFs. Our work provides a faster and precise method to obtain IRF, which may find various FLIM-based applications. We also reported in which conditions a measured or a synthesized IRF can be applied.", keywords = "time-resolved imaging, photon counting, deconvolution, fluorescence microscopy, medical and biological imaging, instrument response function", author = "Dong Xiao and Natakorn Sapermsap and Mohammed Safar and Cunningham, {Margaret Rose} and Yu Chen and Li, {David Day-Uei}", year = "2021", month = mar, day = "2", doi = "10.3389/fphy.2021.635645", language = "English", volume = "9", journal = "Frontiers in Physics", publisher = "Frontiers Media", } . Frontiers in Physics.

MOHAMMED SAFAR, Dong Xiao, Natakorn Sapermsap, Margaret Rose Cunningham, Yu Chen, David Day-Uei Li(2021). On Synthetic Instrument Response Functions of Time-Correlated Single-Photon Counting Based Fluorescence Lifetime Imaging Analysis . Frontiers in Physics. 9. (ARTN 635645). FRONTIERS MEDIA SA

MOHAMMED SAFAR, Yahui Li, Sapermsap Natakorn, Yu Chen, Margaret Cunningham, Jinshou Tian, David Day-Uei Li(2021). Corrigendum: Investigations on Average Fluorescence Lifetimes for Visualizing Multi-Exponential Decays (vol 8, 576862, 2020) . Frontiers in Physics. 8. (ARTN 637953). FRONTIERS MEDIA SA

MOHAMMED SAFAR, Yahui Li, Sapermsap Natakorn, Yu Chen, Margaret Cunningham, Jinshou Tian, David Day-Uei Li(2020). Investigations on Average Fluorescence Lifetimes for Visualizing Multi-Exponential Decays . Frontiers in Physics. 8. (ARTN 576862). FRONTIERS MEDIA SA

Investigations on average fluorescence lifetimes for visualizing multi-exponential decays @article{db6a343b7d5744d7974a9c1484c25186, title = "Investigations on average fluorescence lifetimes for visualizing multi-exponential decays", abstract = "Intensity- and amplitude-weighted average lifetimes, denoted as τ I and τ A hereafter, are useful indicators for revealing F{\"o}rster resonance energy transfer (FRET) or fluorescence quenching behaviors. In this work, we discussed the differences between τ I and τ A and presented several model-free lifetime determination algorithms (LDA), including the center-of-mass, phasor, and integral equation methods for fast τ I and τ A estimations. For model-based LDAs, we discussed the model-mismatch problems, and the results suggest that a bi-exponential model can well approximate a signal following a multi-exponential model. Depending on the application requirements, suggestions about the LDAs to be used are given. The instrument responses of the imaging systems were included in the analysis. We explained why only using the τ I model for FRET analysis can be misleading; both τ I and τ A models should be considered. We also proposed using τ A/τ I as a new indicator on two-photon fluorescence lifetime images, and the results show that τ A/τ I is an intuitive tool for visualizing multi-exponential decays. ", keywords = "fluorescence lifetime imaging, lifetime determination algorithm, average lifetimes, multi-exponential decays, lifetime image visualization", author = "Yahui Li and Sapermsap Natakorn and Yu Chen and Mohammed Safar and Margaret Cunningham and Jinshou Tian and Li, {David Day-Uei}", year = "2020", month = oct, day = "16", doi = "10.3389/fphy.2020.576862", language = "English", volume = "8", journal = "Frontiers in Physics", publisher = "Frontiers Media", } . Frontiers in Physics.

CONFERENCE POSTER

The functional relevance of P2Y1 and P2Y12 receptor heterodimerization @conference{d9175c95ac9d424e9e4ff153d972de06, title = "The functional relevance of P2Y1 and P2Y12 receptor heterodimerization", abstract = "Introduction: ADP is an endogenous agonist for some G protein-coupled receptors (GPCRs) such as P2Y1 and P2Y12 purinoceptors. Previous studies demonstrated that AR-C69931MX, which is P2Y12 antagonist, inhibits ADP-induced intracellular Ca2+ in recombinant P2Y1 and P2Y12 receptors. In this study we examined the effect of AR-C69931MX on native P2Y1 receptor signaling. Also, test the physical interaction between both receptors in the recombinant and native system. Method: tSA201 cells, which are a transformed human kidney cell line, were transfected or co-transfected with hP2Y1 and hP2Y12 receptors tagged with HA (N-terminal) or a fluorescent protein (C-terminal). Other experiments used BV-2 cells, which are mouse microglial cells. The combination of lifetime and FRET (FLIM-FRET) technique using (CFP/YFP tagged receptors) was used to detect the physical interaction for P2Y1-P2Y12 heterodimerization in the recombinant system, while proximity ligation assay (PLA) used to determine the heterodimer in the recombinant and native system. Intracellular Ca2+ influx was determined using Cal-520 dye in FlexStation Microplate Reader.Result: In tSA201 cells, PLA indicated that the physical interaction for both receptors locate mainly on the cell membrane (n=3). The measured fluorescence lifetime in cells transfected only with the donor (P2Y12-eCFP) (1.55 ns) was significantly higher compared to cells co-transfected with the acceptor (P2Y1-eYFP) (2.21 ns), providing a strong evidence for P2Y1-P2Y12 dimerization (n=3). In BV-2 cells, PLA detected the interaction between both receptors natively, which was located intracellularly (n=3). Interestingly, AR-C69931MX (1 μM) significantly reduced the ADP (300nM)-induced Ca2+ influx in the BV-2 cells (n=4).Conclusion: P2Y1 and P2Y12 heterodimer locates on the cell membrane in the recombinant system while it locates intracellularly in the native system. Native P2Y1 receptor signaling inhibited using P2Y12 antagonist, which similar finding from the Kennedy lab that used recombinant system. Further work in under way to investigate the interaction between both receptors in disease models, and investigate the signaling relevance for the formed dimer.", keywords = "G protein-coupled receptors, GPCRs, heterodimerization", author = "Moa Safar", year = "2020", month = dec, day = "14", language = "English", note = "Pharmacology 2020 ; Conference date: 14-12-2020 Through 19-12-2020", } . Pharmacology 2020, Online, 14/12/20.

Interrogating purinergic P2Y1 and P2Y12 heterodimerisation @conference{d56ca69021c4440e967080c5f0b85aa2, title = "Interrogating purinergic P2Y1 and P2Y12 heterodimerisation", abstract = "ADP is an endogenous agonist for some G protein-coupled receptors (GPCRs) such as P2Y1 and P2Y12 purinoceptors. Previous studies demonstrated that AR-C69931MX, which is P2Y12 antagonist, inhibits ADP-induced intracellular Ca2+ in recombinant P2Y1 and P2Y12 receptors. In this study, we examined the effect of AR-C69931MX on native P2Y1 receptor signalling. Also, test the physical interaction between both receptors in the recombinant and native system. In the recombinant system (tSA201 cells), the physical interaction between the receptors was determined using co-immunoprecipitation (co-IP), proximity ligation assay (PLA) and the combination of lifetime and FRET (FLIM-FRET) technique that was developed and optimised with the cooperation with the physics department at the University of Strathclyde1. While in the native system (BV-2 microglial cells), PLA was used to determine the physical interaction. To investigate the influence of this dimer on receptors function, we measured the intracellular Ca2+ influx using Cal-520 dye in FlexStation Microplate Reader. We found that P2Y1 and P2Y12 can form a heterodimer that locates on the cell membrane in the recombinant system while it locates intracellularly in the native system. Native P2Y1 receptor signalling inhibited using P2Y12 antagonist, which similar finding from the Kennedy lab that used a recombinant system. Further work in underway to investigate the interaction between both receptors in disease models, and investigate the signalling relevance for the formed dimer.", keywords = "heterodimerisation, G protein-coupled receptors, antagonist", author = "Mohammed Safar and Rothwelle Tate and Natakorn Sapermsap and David Li and Margaret Cunningham and Charles Kennedy", year = "2020", month = oct, day = "14", language = "English", note = "3rd ERNEST Conference ; Conference date: 12-10-2020 Through 14-10-2020", } . 3rd ERNEST Conference, Online, 12/10/20.

Heterodimerisation of purinergic GPCRs @conference{582d110cf8e74d7e82657761ee78800f, title = "Heterodimerisation of purinergic GPCRs", keywords = "G protein coupled receptors (GPCR), receptor interaction, recombinant systems", author = "Safar, {Mohammed Adnan A} and Wood, {Rachel A} and Cunningham, {Margaret R} and Charles Kennedy", year = "2018", month = nov, day = "15", language = "English", note = "Molecular Neuropharmacology in Health and Wellbeing : Exploring new targets for drug discovery ; Conference date: 15-11-2018 Through 15-11-2018", url = "https://www.eventbrite.co.uk/e/young-life-scientists-symposium-2018-tickets-48550238069?aff=ebdssbdestsearch#", } . Molecular Neuropharmacology in Health and Wellbeing, Glasgow, United Kingdom, 15/11/18.

Evidence that human P2Y1 and P2Y12 receptors form heterodimers @conference{64f88dfc4a104dadbc7757fddff00f6a, title = "Evidence that human P2Y1 and P2Y12 receptors form heterodimers", abstract = "Introduction: P2Y1 and P2Y12 receptors belong to the class A family of transmembrane GPCRs that are activated by endogenous nucleotides1. There is growing evidence that many GPCRs, including P2Y receptors, can exist as dimers or higher-order oligomers2. For example, P2Y12 and PAR4 receptors were recently reported to dimerise3. Our previous studies indicated that hP2Y1 and hP2Y12 receptors may form a functional heterodimer with novel pharmacological and signalling properties4. The aim of this project was, therefore, to characterise the physical interaction between hP2Y1 and hP2Y12 receptors.Method:tSA201 cells were transfected or co-transfected with hP2Y1 and hP2Y12 receptors, tagged with HA or a fluorescent protein. Cellular localisation and co-localisation of the receptors were determined using confocal microscopy. Transfected cells were cultured in the absence or presence of the N-glycosylation inhibitor tunicamycin (2.0 μg/ml) for 16 hours to determine the role of N-glycosylation in receptors expression. Receptor cell surface expression was quantified using ELISA. To investigate physical interaction between the two P2Y subtypes, co-immunoprecipitation was performed using anti-HA-agarose beads followed by immunoblotting with anti-GFP, anti-HA then alpha-Tubulin antibodies.Result: Following transfection on their own or together, both receptors were localised mainly at the cell membrane, and this was unaffected by tunicamycin. Co-immunoprecipitation confirmed that P2Y1 and P2Y12 receptors associate physically. Each subtype enhanced the other's surface expressions. In particular, expression of the P2Y12 receptor more than doubled that of P2Y1 receptors at the cell surface.Conclusion: These results show that P2Y1 and P2Y12 receptors are physically associated at the cell membrane and that they enhance each other's cell surface expressions. These results are consistent with our previous data indicating that P2Y1 and P2Y12 receptors form a functional heteromer.References:1. Kennedy C et al (2013) Future Med Chem 5: 431-449.2. Milligan G, (2013) Mol Pharmacol 84: 158-169.3. Smith T. H. et al. (2017) J Biol Chem 292(33): 13867-13878.4. Shakya-Shrestha S et al. (2010) Mol.Cell Neurosci 43: 363-369.", keywords = "P2Y1, P2Y12, functional heteromer", author = "M. Safar", year = "2018", month = may, day = "17", language = "English", note = "Pharmacology Futures 2018 : Celebrating 250 Years of Pharmacology in Edinburgh ; Conference date: 17-05-2018 Through 17-05-2018", url = "http://www.pa2online.org/abstract/abstract.jsp?abid=33713&author=safar&cat=-1&period=-1", } . Pharmacology Futures 2018, Edinburgh , United Kingdom, 17/05/18.

DISSERTATION THESIS

MOHAMMED SAFAR, Charles Kennedy, Margaret Cunningham(2020). Understanding the pharmacological consequence of functional P2Y1- P2Y12 heterodimerisation.

MOHAMMED SAFAR, Sharron Dolan(2015). How does oxycodone work?.

CONFERENCE PAPER

E Fagbodun, A Osman, S Zuffa, J Swann, A Bailey(2019). Effect of A1 versus a2™ milk exposure at an early developmental age on the endogenous opioid system of the rat brain . British Journal of Pharmacology. 176. (16). p. 2980--2981. Wiley

MOHAMMED SAFAR, R Wood, M R Cunningham, C Kennedy(2019). P2Y₁ and P2Y₁₂ receptor heterodimerisation: From recombinant systems to native detection. British Journal of Pharmacology. 176. (16). p. 3049--3049. WILEY

MOHAMMED SAFAR, C J McMullen, C McCluskey, S J Kim, S Laovitthayanggoon, M MacDonald, R Wood, M R Cunningham, S Currie(2018). ANTI-CANCER TYROSINE KINASE INHIBITORS INCREASE OXIDATIVE STRESS IN PRIMARY CARDIAC FIBROBLASTS . Heart. 104. p. A9--A9. BMJ PUBLISHING GROUP

OTHER

P2Y1 and P2Y12 receptor heterodimerisation @article{e7a711c3b1df4bbaa17a4d70db7fee97, title = "P2Y1 and P2Y12 receptor heterodimerisation: from recombinant systems to native detection", abstract = "Purinergic P2Y1 and P2Y12 receptors belong to the class A family of transmembrane G‐protein coupled receptors (GPCRs) and have been demonstrated to exist as homodimers and oligomers and form heterodimers with other GPCRs. P2Y12 and protease‐activated receptor 4 (PAR4) were recently reported to form a heterodimer with implications in receptor trafficking and signalling. Our unpublished studies suggest that hP2Y1 and hP2Y12 heterodimerise; therefore, the aim of this study was to investigate the functional relevance of receptor interaction, firstly in recombinant systems and then natively in microglial cells. hP2Y1 and hP2Y12 receptor heterodimersation impacted ADP‐mediated internalisation when both receptors are overexpressed in tSA201 cells. Co‐localisation studies in BV‐2 cells suggest that the location of receptor interaction may differ depending upon the cell types explored. Further work is under way to investigate these differences.", keywords = "P2Y1 receptors, P2Y12 receptors, G‐protein coupled receptors (GPCRs), heterodimersation", author = "M.A. Safar and R. Wood and M.R. Cunningham and C. Kennedy", note = "Abstract number: OC053. ; Pharmacology 2018 ; Conference date: 18-12-2018 Through 20-12-2018", year = "2019", month = aug, day = "1", doi = "10.1111/bph.14681", language = "English", volume = "176", pages = "3049", journal = "British Journal of Pharmacology", issn = "0007-1188", publisher = "John Wiley and Sons Inc.", number = "16", url = "https://www.bps.ac.uk/news-events/events/2018/december/pharmacology-2018", } . British Journal of Pharmacology.

Anti-cancer tyrosine kinase inhibitors increase oxidative stress in primary cardiac fibroblasts @article{87a8c79303dd439c82466229fc31dddd, title = "Anti-cancer tyrosine kinase inhibitors increase oxidative stress in primary cardiac fibroblasts", abstract = "Anti-cancer tyrosine kinase inhibitors (TKI) are known to exert cardiotoxicity that can result in heart failure. Here we have used primary adult rat cardiac fibroblasts (CFs) to examine whether imatinib and sunitinib (both TKIs) increase oxidative stress and cause increased oxidation and activation of calcium/calmodulin dependent protein kinase II (CaMKII). Activation of CaMKII is known to be important for cellular function but excessive activation is linked to cardiac pathology. CFs, isolated from adult Wistar rat hearts, were maintained in culture and treated over 24 hour with the TKIs sunitinib and imatinib (0.1–20 µM) in serum-free medium (DMEM). Cell phenotype and growth was monitored using a Nikon Eclipse (TE300) inverted microscope and ROS assays performed using a specially designed assay kit (Abcam, UK) which uses DCFDA to measure hydroxyl, peroxyl and other ROS activity. Quantitative immunoblotting was used to assess ox-CaMKII protein levels. Treatment with both TKIs caused a dose-dependent decrease in cell viability. Sunitinib exerted more toxic effects at lower concentrations than imatinib. Decreased cell viability was evident at concentrations as low as 1 µM for sunitinib with dramatic cell loss (>50%) evident at 10–20 µM. Significantly increased ROS levels (using the DFCDA-based assay) were observed in the presence of both imatinib (4956±102 vs 1984±358 (imatinib vs vehicle (a.u.), n=3, p<0.05) and sunitinib (15186±3856 vs 1984±358 (sunitinib vs vehicle (a.u.), n=3, p<0.01). Quantitative immunoblotting suggested that ox-CaMKII levels were increased following treatment with either 1 µM imatinib (1.4-fold (ox-CaMKII/GAPDH)) or 1 µM sunitinib (1.2-fold (ox-CaMKII/GAPDH)) however at higher concentrations (particularly for sunitinib) increased cell loss and resultant loss of total protein was observed. In conclusion, both imatinib and sunitinib cause increased oxidative stress in adult primary CFs with resultant activation of CaMKII. These effects are evident at lower concentrations of sunitinib than for imatinib and reflect the increased cardiotoxicity of this TKI reported in the patient.", keywords = "TKIs, heart failure, cardiotoxicity", author = "CJ McMullen and C McCluskey and SJ Kim and S Laovitthayanggoon and M MacDonald and M Safar and R Wood and MR Cunningham and S Currie", year = "2018", month = mar, day = "26", doi = "10.1136/heartjnl-2018-SCF.22", language = "English", volume = "104", journal = "Heart ", issn = "1355-6037", publisher = "BMJ Publishing Group", number = "S4", note = "The Scottish Cardiovascular Forum 2018 ; Conference date: 03-02-2018 Through 03-02-2018", } . Heart.

CONFERENCE ABSTRACT

P2Y1 and P2Y12 receptor heterodimerisation @conference{7830fa4291fd41ca83cac69737cf3f98, title = "P2Y1 and P2Y12 receptor heterodimerisation: from recombinant systems to native detection", abstract = "Purinergic P2Y1 and P2Y12 receptors are G protein-coupled receptors (GPCRs) that have been demonstrated to dimerise with other GPCRs. Our unpublished studies suggest that hP2Y1 and hP2Y12 heterodimerise therefore the aim of this study was to investigate the functional relevance of receptor interaction, firstly in recombinant systems and then natively in microglial cells.tSA201 cells, which are a transformed human kidney cell line, were transfected or co-transfected with hP2Y1 and hP2Y12 receptors. Their cellular co-localisation was determined using confocal microscopy and physical interaction by co-immunoprecipitation. Cell surface expression and receptor trafficking was quantified using surface ELISA approach. Native P2Y receptors were detected in mouse BV-2 microglial cells using RT-PCR and indirect immunofluorescence.Previous co-immunoprecipitation experiments revealed that P2Y1 and P2Y12 receptors heterodimerisation. This study shows that hP2Y1 and hP2Y12 receptors express predominantly at the cell surface in tSA201 cells. hP2Y12 receptor expression was reduced by 22.5{\%} (n=3), at the cell surface when co-expressed with hP2Y1, but not vice-versa. hP2Y1 and hP2Y12 internalization to ADP (0-60mins, 10µM) was maximum 30 min post-treatment (28.8{\%} ±6.2 and 20.8{\%} ±7.8, respectively). When receptors were co-expressed, ADP did not reduce receptor surface expression (n=3). Interestingly, native P2Y1 and P2Y12 receptors in BV-2 cells also appear to co-localise with Pearson's correlation coefficient =0.684 ±0.004 (n=3, 200 cells), however signals were detected intracellularly rather than at the cell surface.hP2Y1 and hP2Y12 receptor heterodimersation impacted ADP-mediated internalisation when both receptors were overexpressed in tSA201 cells. Co-localisation studies in BV-2 cells suggest that the location of receptor interaction may differ depending upon the cell types explored. Further work is under way to investigate these differences.", keywords = "heterodimerisation, receptor heterodimerisation, Purinergic P2Y1 receptors, Purinergic P2Y12 receptors", author = "Safar, {Mohammed Adnan A} and Wood, {Rachel Aimee} and Rothwelle Tate and Cunningham, {Margaret Rose} and Charles Kennedy", year = "2018", month = "12", day = "2", language = "English", note = "BPS-MPGPCR 2018 ; Conference date: 02-12-2018 Through 04-12-2018", url = "https://www.monash.edu/pharm/about/events/BPS-MPGPCR-Meeting-2018", } . BPS-MPGPCR 2018, Melbourne, Australia, 2/12/18.