Contribute in developing different versions of a variety of programs that control laboratory instruments (mainly Spark Cyto) for biopharmaceutical and clinical applications, and analyze results and cell images of measurements. The used technologies are C# .Net and C++ (with OpenCV).

08.2018 – Present

Contributed in developing a 3D social networking application (Connect) that works on Windows and Android devices. The used technologies were C# .Net Core for the server-side, and Unity for the front-end. I also managed the internal and production servers and networks of the company. The servers were Linux servers (as Domain Controller using Samba), with different services (e.g. RocketChat, VeraCrypt, NGinx, Apache and LetsEncrypt).

09.2015 – 12.2017

Dissertation (Ph.D. Thesis): Cellular Type-Specific Tetrahydrobiopterin Recycling by Dihydrofolate Reductase.

Tetrahydrobiopterin (BH4) is a key cofactor of endothelial nitric oxide synthase (eNOS) that drives formation of nitric oxide (NO), rather than superoxide, and thus plays an important role in endothelial cell function and blood pressure regulation. BH4 can be recycled by dihydrofolate reductase (DHFR), which seems to be important for BH4 bioavailability in some species. A previous study indicated that BH4 recycling efficiency (particularly the binding affinity) is significantly greater in porcine endothelial cells than in human endothelial cells, but the mechanisms were unclear. Here, we investigated the underlying mechanism(s) of enhanced BH4 recycling efficiency in porcine cells. We found that purified recombinant porcine DHFR exhibits significantly higher affinity for BH2 substrate than recombinant human DHFR. We next tried to identify species-specific differences in DHFR structure that contribute to the high affinity of porcine DHFR for BH2. We introduced 4 targeted mutations within or outside of the active site of human DHFR, replacing the human amino acid residues with the corresponding porcine residues (F32Y/R33K/G70D/K55R). Human DHFR affinity for BH2 was improved by the F32Y/R33K and K55R mutation, but was still weaker than porcine DHFR. The studied mutations caused unexpected differences in the catalytic activity of DHFR, particularly for dihydrofolate (FH2) substrate. Based on the 3D structure of DHFR, we discuss how the targeted amino acid substitutions could alter DHFR-substrate and DHFR-cofactor hydrogen bond formation and change the pKa of molecules in the substrate and DHFR structure. Taken together, our findings identify F32Y/R33K as an important element in DHFR binding affinity for BH2 substrate, and suggest additional more distal amino acid differences (K55R in our study) also likely play a role in enhanced porcine DHFR activity.

01.2014 – 02.2018

Created and managed the #1 pharmaceutical forum (Elixir) in Aleppo, Syria, which was tightly related to the news of the Faculty of Pharmacy – Aleppo University. In addition to managing the website technically, I led the whole team of moderators of the forum. The used technologies were vBulletin, Joomla, PHP, HTML and CSS.

Unfortunately, because of the war situation which led to unreliable internet-access, many students and members were not able to surf the website anymore. Consequently, I decided later to shut the website down.

Archive link (2011):

2009 – 2013