Dr.

 

                                   
S. Mohsen Asghari
Associate Professor of Biochemistry
Tel: +98-21 66969257
E-mail: sm.asghari@ut.ac.ir
 
     

   

  Dr. S. Mohsen Asghari was born in 1978, in Tehran. He was graduated in Professor Hesabi high school in Tehran (1996), received his B.Sc. in Biology-Animal Sciences from Gorgan University of Agricultural Sciences, Gorgan (2000), and his M.Sc. (2003) and Ph.D. (2008) in Biochemistry from Tarbiat Modares University, Tehran, Iran. During M.Sc. and Ph.D., the focus of his studies was on the structure-function relationships of enzymes and rational protein engineering. After a sabbatical in Utrecht University, the Netherlands, he was joined the University of Guilan at 2009 as assistant professor. Dr Asghari was promoted to associate professor of biochemistry in 2017 and, since 2020, he has joined to IBB.

He is teaching enzymology, cell signaling and biochemistry of cancer for M.Sc. and Ph.D. students of IBB, enzymology for Ph.D. students of biotechnology (College of Science), and advanced biochemical engineering for Ph.D. students of biotechnology (School of Chemical Engineering).

Dr. Asghari's group aims to find and develop the novel vascular endothelial growth factor receptor (VEGFR)-targeting peptides to combat pathological angiogenesis in tumors and major blinding retinal diseases such as aged macular degeneration (AMD), and improve tumor imaging. Moreover, nanomedicinal systems are being used to combine cancer treatment and tumor imaging. His Lab., Biochemical Engineering Lab., has close collaborations with Tehran University of Medical Sciences Preclinical Core Facility, Tehran University of Medical Sciences Faculty of Pharmacy, Shahid Beheshti University of Medical Sciences Ophthalmic Research Center and KNTU Peptide Synthesis Lab.


                                                                                                                                     

CV

 

Personal Records                                                

  

Education

  
 

Name: S. Mohsen Asghari

Date of Birth: 1978/01/20

Place of Birth: Tehran, Iran

Marital Status: Married, two children

Office Address: Institute of Biochemistry and Biophysics, University of Tehran

Phone Number: +9821 61113451

Fax: +98 21 66404680 

Email: sm.asghari@ut.ac.ir

Web site: https://ibb.ut.ac.ir/en/asghari

  

B.Sc.: Gorgan University of Agricultural Sciences, Gorgan, Iran (2000)

Major: Biology-Animal Sciences

M.Sc.: Tarbiat Modares University, Tehran, Iran (2003)

Major: Biochemistry

Ph.D.: Tarbiat Modares University, Tehran, Iran (2008)

Major: Biochemistry

Thesis Title: Improvement of activity and stability of a protease from a native bacterium by site-directed mutagenesis

 
  

 

Research Interests:

Receptor tyrosine kinases (RTKs) are key molecules in numerous cellular processes, the inhibitors of which play an important role in the clinic. Among them are the vascular endothelial growth factor (VEGF) family members and their receptors (VEGFRs), which are essential in the formation of new blood vessels by angiogenesis. Angiogenesis underlies many severe diseases including different cancers and major blinding retinal diseases such as aged macular degeneration (AMD). This observation has driven development of specific inhibitors that block a central factor in tumor growth and AMD, VEGF, from binding to its receptors VEGFR-1 and mainly VEGFR-2. In Biochemical Engineering Lab., we focus on the designing and characterization of small peptidomimetics that target the extracellular ligand-binding domain of both VEGFR1 and VEGFR2. These peptides specifically prevent the binding of VEGF family members to their receptors and downstream signaling. VEGFR-targeting peptides can serve as theranostic agents (i.e. applicable for both therapeutic and diagnostic purposes) in oncology and ophthalmology. An important aspect in our strategy is dual blockade of VEGFR1 and VEGFR2, resulting in greater targeting efficiency and, consequently, more effective inhibition of angiogenesis. We also apply nanomedicinal approaches to enhance the functional properties and the circulation half-life of the peptides, and/or to combine the cancer treatment with tumor imaging. In this regard, we are currently working on nanoalbumin (NAB)-based drug delivery, solid lipid nanoparticles (SLNs) and gold nanoparticles.

Projects:

  1. Improvement of the receptor binding property of the peptides. Given that the binding affinity is a critical aspect in the application of the targeting molecules, we devote considerable efforts to enhance the binding affinity (decreasing the dissociation constant (Kd)) of the peptides toward the ectodomain of VEGFRs.
  2. Application of the VEGFR-targeting peptides for treatment of cancer. To assess the antitumor effects of peptides, different in vitro and in vivo experiments are being used. The in vitro characterizations, using human umbilical vein endothelial (HUVE) and/or different tumoral cell lines, include cell proliferation, migration, angiogenesis, apoptosis induction and the downstream signaling pathways of VEGFRs. The in vivo studies are carried out in animal research facility of IBB. In this core facility, extensive animal studies in the field of translational medicine are carried out. To this end, we deliver the peptides in tumor-bearing animal models alone or in combination with chemotherapeutics via direct injection or using nanosystems, including nanoalbumin (NAB), solid lipid nanoparticles (SLNs) and gold nanoparticles, and evaluate the efficacy of treatments. In collaboration with the Tehran University of Medical Sciences Preclinical Core Facility, we use animal-PET, micro-CT and animal-SPECT to investigate the biodistribution and anti-metastatic potential of our therapeutics.
  3. Application of VEGFR-targeting peptides for treatment of aged macular degeneration (AMD). In this project, in collaboration with Shahid Beheshti University of Medical Sciences Ophthalmic Research Center, we aim to apply our anti-angiogenic peptides for treatment of the neovascular angiogenesis in AMD. Accordingly, besides in vitro studies, the animal models of AMD are treated by the peptides via either intraperitoneal injection or eye drops.
  4. Designing and characterization of the peptide-based contrast agents for imaging of breast and brain tumors. In this project, funded by National Institute for Medical Research Development (NIMAD), we use our VEGFR-binding peptides, e.g. as peptide-DTPA-Gd or peptide-DTPA-Ga68, for contrast enhancement in MRI and PET imaging, respectively, using animal models of breast and brain tumors.

 

 

Publications

 

Full International Papers

*: the corresponding author

  1. H. Allahmoradi, S.M. Asghari*, A. Ahmadi. E. Assareh, M. Nazari. Anti-tumor and anti-metastatic activity of the FGF2 118-126 fragment dependent on the loop structure. Biochemical Journal (2022) 479, 1285-1302.

 

  1. P. Zanjanchi, S.M. Asghari*, H. Mohabatkar, M. Shourian, M. Shafiee Ardestani. Conjugation of VEGFR1/R2-targeting peptide with gold nanoparticles to enhance antiangiogenic and antitumoral activity. Journal of Nanobiotechnology (2022) 20 (1), 1-22.

 

  1. P. Shakeri, S.M. Asghari, E. Panahi Kokhdan, V. Fathi Vavsari, F. Golmohammadi, A. Ghassempour, S. Balalaie*. Synthesis, molecular modeling and functional evaluation of a GnRH antagonist. Journal of the Iranian Chemical Society (2022) 19, 2705-2717.

 

  1. M. F. Behelgardi, Z. Gholami Shahvir, S.M. Asghari. Apoptosis induction in human lung and colon cancer cells via impeding VEGF signaling pathways. Molecular Biology Reports (2022) 49, 3637-3647.

 

  1. HR Rudmianeh, M Shourian*, R Ansari*, FG Pirbasti, SM Asghari. Polysaccharide Nanogels for the Delivery of Gemcitabine Hydrochloride. ACS Applied Polymer Materials (2021) 3 (12), 6345-6358.

 

  1. A. Valipour, B. Heidari*, S.M. Asghari, S. Balalaie, H. Rabouti, N. Omidian. Expression of reproductive related genes and changes in oocyte maturation of goldfish broodstock (Carassius auratus) following injection of different exogenous kisspeptins. Reproduction in Domestic Animals (2021) 56 (10), 1349-1357.

 

  1. A. Valipour, B. Heidari*, S.M. Asghari, S. Balalaie, H. Rabouti, N. Omidian. The effect of different exogenous kisspeptins on sex hormones and reproductive indices of the goldfish (Carassius auratus) broodstock. Fish Biology (2021), 98(4):1137-1143.

 

  1. A. Sadremomtaz, A.M. Ali, F. Jouyandeh, S. Balalaie, R. Navari, S. Broussy, K. Mansouri, M.R. Groves*, S.M. Asghari*. Molecular docking, synthesis and biological evaluation of Vascular Endothelial Growth Factor (VEGF) B based peptide as anti-angiogenic agent targeting the second domain of the Vascular Endothelial Growth Factor Receptor 1 (VEGFR1D2) for anticancer application. Signal Transduction and Targeted Therapy (2020), 5:76.

 

  1. E. Assareh, F. Mehrnejad, S. Mohsen Asghari*. Structural Studies on an Anti-angiogenic Peptide Using Molecular Modeling. Iranian Journal of Biotechnology (2020). 2020;18(4): e2553.

 

  1. M.F. Behelgardi, S. Zahri, Z. Gholami Shahvir, F. Mashayekhi, L. Mirzanejad, S.M. Asghari*. Targeting signaling pathways of VEGFR1 and VEGFR2 as a potential target in the treatment of breast cancer. Molecular Biology Reports (2020) 47: 2061-2071

 

  1. N. Rezaei, F. Mehrnejad*, Z. Vaezi, M. Sedghi, S.M. Asghari, H. Naderi-Manesh*. Encapsulation of an endostatin peptide in liposomes: Stability, release, and cytotoxicity study. Colloids and Surfaces B Biointerfaces (2020) 185:110552.

 

  1. R. Chamani, H. Soleimanjahi*, S.M. Asghari, H. Karimi, Z. Kianmehr, S.K. Ardestani. Re-engineering of the immunosuppressive tumor microenvironment by antiangiogenic therapy. International Journal of Peptide Research and Therapeutics (2020) 26: 539-546.

 

  1. E. Assareh, F. Mehrnejad, K. Mansouri, A.R. Esmaeili Rastaghi, H. Naderi-Manesh, S.M. Asghari*. A cyclic peptide reproducing the α1 helix of VEGF-B binds to VEGFR-1 and VEGFR-2 and inhibits angiogenesis and tumor growth. Biochemical Journal (2019) 476: 645-663

 

  1. A. Sadremomtaz, F. Kobarfard, K. Mansouri, L. Mirzanejad, S.M. Asghari*. Suppression of migratory and metastatic pathways via blocking VEGFR1 and VEGFR2. Journal of Receptors and Signal Transduction (2019) 38(5-6):432-441.

 

  1. M. Farzaneh Behelgardi, S. Zahri*, F. Mashayekhi, K. Mansouri, S.M. Asghari*. A peptide mimicking the binding sites of VEGF-A and VEGF-B inhibits VEGFR-1/-2 driven angiogenesis, tumor growth and metastasis. Scientific Reports (2018) 8(1): 17924.

 

  1. F. Hamdan, Z. Bigdeli, S.M. Asghari, A. Sadremomtaz, S. Balalaie*. Synthesis of modified RGD based peptides and their in vitro activity. ChemMedChem (2018) 14, 282-288. 

 

  1. A. Sadremomtaz, K. Mansouri, G. Alemzadeh, M. Safa, A.E. Rastaghi, S.M. Asghari*. Dual blockade of VEGFR1 and VEGFR2 by a novel peptide abrogates VEGF-driven angiogenesis, tumor growth, and metastasis through PI3K/AKT and MAPK/ERK1/2 pathway. Biochimica et Biophysica Acta-General Subjects (2018) 1862: 2688-2700.

 

  1. M. Jafari, F. Mehrnejad*, F. Rahimi, and S.M. Asghari. The molecular basis of the sodium dodecyl sulfate effect on human ubiquitin structure: A molecular dynamics simulation study. Scientific Reports (2018) 8(1): 2150.

 

  1. M. Jafarzadeh, K. Mousavizadeh, M.T. Joghataei, M.H. Bahremani, M. Safa, S.M. Asghari*. Effect of designed fibroblast growth factor antagonistic peptide on the inhibition of angiogenesis in Balb/c mice with breast cancer. Open Life Sciences (2018) 13: 348-354.

 

  1. S. Ebrahimi Samani, Z. Seraj, H. Naderimanesh, K. Khajeh, A.R. Esmaeili Rastaghi, T. Droudi, P. Kolivand, H. Kazemi, S.M. Asghari*. Controlled release of an endostatin peptide using chitosan nanoparticles. Chemical Biology & Drug Design (2017) 90: 417-424.

 

  1. M. Salehi, M.R. Aghamaali*, R.H. Sajedi, S.M. Asghari, E. Jorjani. Purification and characterization of a milk-clotting aspartic protease from Withania coagulans fruit. International Journal of Biological Macromolecules (2017) 97: 847-854.

 

  1. P. Saadat, H. Soleimanjahi*, S.M. Asghari, M. Fazeli, H. Razavinikoo, H. Karimi. Co-administration of anti-angiogenic peptide and DNA vaccine in cervical cancer tumor model. International Journal of Cancer Management (2017) 10(3): e4723 doi: 10.5812/ijcm.4723.

 

  1. S.M. Asghari*, M. Isazadeh, M. Taghdir. The relevance of low affinity Ca-binding sites to the structure, stability and kinetic properties of thermolysin. Journal of the Iranian Chemical Society (2016) 13: 1887-1894.

 

  1. M. Halimi, A. Shahabi, D. Moslemi, H. Parsian*, S.M. Asghari*, R. Sariri, F. Yeganeh, E. Zabihi. Human serum miR-34a as an indicator of exposure to ionizing radiation. Radiation and Environmental Biophysics. (2016) 55: 423-429.

 

  1. R. Chamani, S.M. Asghari*, A. M. Alizadeh, R. Khodarahmi, T. Doroudi, P.H. Kolivand, H. Ghafouri, H. Rabouti. The antiangiogenic and antitumor activities of the N-terminal fragment of endostatin augmented by Ile/Arg substitution: the overall structure implicated the biological activity. Biochimica et Biophysica Acta-Proteins and Proteomics (2016) 1864: 1765-1774.

 

  1. S. Esmaeili, M.R. Ashrafi Kooshk, S.M. Asghari, R. Khodarahmi*. Heme-coordinated histidine residues formnon-specific functional "ferritin-heme" peroxidase system: possible and partial mechanistic relevance to oxidative stress-mediated pathology in neurodegenerative diseases. International Journal of Biological Macromolecules (2016) 91: 368-380.

 

  1. Z. Takalloo, R.H. Sajedi*, Saman Hosseinkhani, S.M. Asghari. Real-time monitoring of artemin in vivo chaperone activity using luciferase as an intracellular reporter. Archives of Biochemistry and Biophysics (2016) 610: 33-40.

 

  1. R. Chamani, S.M. Asghari*, A. Gorji, S. Eskandari, R. Khodarahmi, M. Taghdir, K. Mansouri, Z. Heidari, A. Aliakbar, B. Ranjbar, K. Khajeh. Engineering of a disulfide loop instead of a Zn binding loop restores the anti-proliferative, anti-angiogenic and anti-tumor activities of the N-terminal fragment of endostatin: mechanistic and therapeutic insights. Vascular Pharmacology (2015) 72: 73-82.

 

  1. M. Jaafari, M.R. Ashrafi Kooshk, S.M. Asghari, A.A. Moosavi-Movahedi, S. Ghobadi, R. Khodarahmi*. Direct evidence for non-specific peroxidase activity of ‘‘ferritin–heme" complex: possible role in the development of neurodegenerative diseases. Journal of the Iranian Chemical Society (2015) 12: 779-790.

 

  1. M. Halimi, H. Parsian*, S.M. Asghari*, R. Sariri, D. Moslemi, F. Yeganeh, E. Zabihi. Clinical translation of human microRNA 21 as a potential biomarker for exposure to ionizing radiation. Translational Research (2014) 163: 578-584.

 

  1. S.A. Shirdel, K. Khajeh*, S.M. Asghari, and H.R. Karbalaei-Heidari. Enhancement of thermostability and resistance against autolysis in a zinc metalloprotease. Engineering in Life Sciences (2014) 14: 229-234.

 

  1. M. Halimi, H. Parsian*, S.M. Asghari, Reyhane Sariri, Dariush Moslemi, and Farhad Yeganeh. MicroRNAs: Are they indicators for prediction of response to radiotherapy in breast cancer? Journal of Medicinal Hypotheses & Ideas (2013) 7: 59-64.

 

  1. S. Nasrollahi, L. Golalizadeh, R.H. Sajedi*, M. Taghdir, S.M. Asghari, and M. Rassa. Substrate preference of a Geobacillus maltogenic amylase: A kinetic and thermodynamic analysis. International Journal of Biological Macromolecules (2013) 60: 1-9.

 

  1. M. Halimi, S.M. Asghari, R. Sariri, D. Moslemi, H. Parsian*. Cellular response to ionizing radiation: a microRNA story (Review) International Journal of Molecular and Cellular Medicine (2012) 1: 178-84.

 

  1. A. Mahdavi, R.H. Sajedi*, S.M. Asghari, M. Taghdir, and M. Rasa. An Analysis of temperature adaptation in cold-active, mesophilic and thermophilic Bacillus α-amylases. International Journal of Biological Macromolecules (2011) 49: 1038-1045.

 

  1. S.M. Asghari, K. Khajeh*, A. Badoei Dalfard, M. Pazhang, and H.R. Karbalaei-Heidari. Temperature, organic solvent and pH stabilization of the neutral protease from Salinovibrio proteolyticus: significance of the structural calcium. BMB Reports (2011) 44: 665-668.

 

  1. S.M. Asghari, M. Pazhang, S. Ehtesham, H.R. Karbalaei-Heidari, M. Taghdir, M. Sadeghizadeh, H. Naderi-Manesh and K. Khajeh*. Remarkable improvements of a neutral protease activity and stability share the same structural origins. Protein Engineering, Design & Selection (2010) 23: 599-606.

 

  1. A. Badoei-Dalfard, K. Khajeh*, S.M. Asghari, B. Ranjbar, H.R. Karbalaei-Heidari.  Enhanced activity and stability in the presence of organic solvents by increased active site polarity and stabilization of a surface loop in a metalloprotease. Journal of Biochemistry (2010) 148: 231-238.

 

  1. M. Pazhang, K. Khajeh*, S.M. Asghari, H. Falahati and H. Naderi-Manesh. Cloning, Expression, and Characterization of a Novel Methylglyoxal Synthase from Thermus sp. Strain GH5. Applied Biochemistry and Biotechnology (2010) 162: 1519-1528.

 

  1. M. Yazdani, H. Naderi-Manesh*, K. Khajeh, M.R. Soudi, S.M. Asghari, and M. Sharifzadeh. Isolation and characterization of a novel γ-radiation-resistant bacterium from hot spring in Iran. Journal of Basic Microbiology (2009) 49: 1-9.

 

  1. K. Khajeh*, M. Monsef Shokri, S.M. Asghari, F. Moradian, A. Ghasemi, M. Sadeghi, B. Ranjbar, S. Hosseinkhani, S. Gharavi, H. Naderi-Manesh. Acidic and proteolytic digestion of α-amylases from Bacillus licheniformis and Bacillus amyloliquefaciens: stability and flexibility analysis. Enzyme and Microbial Technology (2006) 38: 422-428.

 

  1. S.M. Asghari, K. Khajeh*, B. Ranjbar, R.H. Sajedi, H. Naderi-Manesh. Comparative studies on trifluoroethanol (TFE) state of a thermophilic α-amylase and its mesophilic counterpart: limited proteolysis, conformational analysis, aggregation and reactivation of the enzymes. International Journal of Biological Macromolecules (2004) 34: 173-179.

 

  1. S.M. Asghari, K. Khajeh*, F. Moradian, B. Ranjbar, H. Naderi-Manesh. Acid-induced conformational changes in Bacillus amyloliquefaciens α-amylase: appearance of a molten globule like state. Enzyme and Microbial Technology (2004) 35: 51-57.

 

 

Full National Papers

 

  1. H. Rabouti, S.M. Asghari*, R. Sariri, B. Heidari*, S Balalaei. Determination of Rutilus kutum kisspeptin and its effect on reproductive hormones. Aquatics Physiology and Biotechnology (2022) 9 (4), 1-20.
  2. F Kaboudan, S Talesh Sasani, SM Asghari. The effect of a VEGFB antagonist peptide on the expression level of miR-210 in a mouse model of breast cancer. Nova Biologica Reperta (2021) 8(1): 13-19.
  3. F Amini Sepehr, SM Asghari, M Shourian*. Diagnosis of Anti-Angiogenesis Peptide Binding to HUVECs Using FITC. Armaghane danesh (2019) 24(4): 691-709.
  4. M Salehi, MR Aghamaali*, R Hasansajedi, SM Asghari, E Jorjani. Effect of Metal Ions on Activity, Stability, and Structure of Purified Aspartic Protease from Paneerbad. Modares Journal of Biotechnology (2019) 10(1), 53-60.
  5. SE Samani, SM Asghari*, H Naderimanesh, S Hoseinkhani. Optimization of Preparation of PEG-PLGA Nanoparticles by Solvent Evaporation Method. Modares Journal of Biotechnology (2018) 9(2): 201-205.
  6. AA Varasteh, SM Asghari*, M Taghdir, MR Aghamaali. The relationship of angle between N-and C-terminal domains and the activity of thermolysin and elastase. (2018) 31(1): 114-120.
  7. AA Varsteh, SM Asghari*, M Taghdir, MR Aghamaali, M Pazhang, F Mehrnejad. The effect of calcium on the activation of thermolysin by salt. Cellular and Molecular Researches (Iranian Journal of Biology) (2017) 30(1): 100-105.
  8. M Jafarzadeh, K Mousavizadeh, M Joghataie, SM Asghari*. Effect of Fibroblast Growth Factor Antagonist Peptide on mouse Breast Tumor Growth and Serum Levels of Interleukin-8 and Tumor Necrosis Factor-Alpha. Yafteh (2017) 19 (2), 126-135.
  9. M Isazadeh, SM Asghari*, M Taghdir, A Varasteh, E Assareh. The effect of calcium on the activation of thermolysin by salt. Cellular and Molecular Researches (Iranian Journal of Biology) (2017) 30(1): 100-105.
  10. R Chamani, SM Asghari*. Effects of electrostatic repulsion of positive charges in carboxyl terminal on the structure and interaction of endostatin-derived peptide. Modares Journal of Biotechnology (2016) 7(2): 30-40.
  11. A Sadrmomtaz, SM Asghari*. Comparative studies on the stability of proteases from Pseudomonas aeruginosa against thermolysin from Bacillus thermoproteolyticus in the presence of organic solvents. Cellular and Molecular Researches (Iranian Journal of Biology) (2015) 28(4): 560-567.
  12. N Mokhtarpour, MA Aghamaali*, SM Asghari. Cloning and sequencing xylanase of Anoxybacillus flavithermus from Qinarjeh, Meshkin-Shahr, Iran. Aquatics Physiology and Biotechnology (2015) 3(2): 15-30.
  13. P Najafi, MR Aghamaali*, SM Asghari. A metalloprotease molecular cloning and sequencing of Anoxybacillus flavithermus from Qinarjeh, Meshgin-shahr, Iran. Aquatic Physiology and Biotechnology (2015) 3(3): 83-98.
  14. SM Asghari*, SE Samani, Z Seraj, K Khajeh, S Hoseinkhani. Optimization of chitosan nanoparticles synthesis. Modares Journal of Biotechnology (2014) 4(2): 21-29.
  15. M Kazemi, MR Aghamaali*, SM Asghari, A Varasteh. Biochemical characteristics of alpha amylase produced by Anoxybacillus sp. from Qinarjeh, Meshkin-Shahr. Aquatics Physiology and Biotechnology (2014) 2(2): 17-29.
  16. Z Jahani, M Molakarimi, RH Sajedi*, M Taghdir, S Hoseinkhani, SM Asghari. The role of some amino acid residues in coelenterazine binding site of mnemiopsin compared to coelenterate photoproteins. Modares Journal of Biotechnology (2014) 5(1): 30-40.
  17. S Ehtesham, SM Asghari*. Cloning, Gene Expression, Purification and Characterization of Elastase from Pseudomonas Aeruginosa. New Cellular and Molecular Biotechnology Journal (2012) 2(7): 27-34.
  18. H Rahmani, SM Asghari*, S Ebrahimi, A Sadremomtaz, M Taghdir. Biochemical Characterization of Elastase from Pseodomonas aeruginosa Strain PTCC1430. New Cellular and Molecular Biotechnology Journal (2012) 2(8): 73-77.
  19. A Sadremomtaz, S Ebrahimi, H Rahmani, SM Asghari*, MR Aghamaali, RH Sajedi Reza Hassan Sajedi. Evaluation of protease stability from Pseudomonas aeroginosa strain PTCC1430 in organic solvents. New Cellular and Molecular Biotechnology Journal (2013) 3(9): 85-89.
  20. H. Rahanandeh, G. Khodakaramian, N. Hassanzadeh, A.Seraji, S.M.Asghari and A.R. Tarang. Inhibition of Tea Root Lesion Nematode, Pratylenchus Loosi, by rhizospher bacteria. Journal of Ornamental and Horticultural Plants (Journal of Ornamental Plants) (2011) 2: 243-250.
  21. H. Rahanandeh,G.Khodakaramian, N.Hassanzadeh A. Seraji, and S.M.Asghari. Evaluation of antagonistic Pseudomonas against root lesion nematode of tea. International Journal of Biosciences (2013) 3: 32-40.

 

Courses

Enzymology

Enzymology is the branch of biochemistry aiming to understand how enzymes work through the relationship between structure and function and how they fold into their native state. This multidisciplinary research field integrates areas of biochemistry, microbiology, molecular biology, molecular genetics, and biophysics. In addition, given the therapeutic and commercial success of small-molecule enzyme inhibitors, as exemplified by kinase inhibitors in oncology, a major focus of current drug-discovery and development efforts is on enzyme targets.

Syllabus Details

1) Enzyme classification. 2) Oligomeric enzymes (Advantages of enzyme oligomerization). 3) Transition state theory. 4) Explaining the efficiency of enzyme catalysis. 5) Chemical kinetics. 6) Enzyme active site. 7) Kinetics of one-substrate enzymatic reactions. 8) Methods for plotting initial-rate data. 9) Bisubstrate kinetic mechanisms. 10) Factors affecting the activity of enzymes. 11) Enzyme inhibition. 12) Brief fundamentals of enzyme assay. 13) How calculate the enzyme reaction rate, Km, kcat, kcat/Km, and specific activity. 14) Examples of enzyme mechanism.

Student Learning Outcomes

The major learning objective of the course is to understand the thermodynamic basis of catalysis, theories of enzyme kinetics, the mechanisms of enzyme catalysis, enzyme assay and the mechanisms of enzyme regulation in the cell. At the conclusion of the course students should be able to:

· Describe transition-state theory and Arrhenius equation.

· Describe and use the equations of enzyme kinetics.

· Describe the methods used in enzyme kinetics.

· Describe the principles of enzyme inhibition.

· Describe the mechanisms of enzyme catalysis.

· Describe the determination of enzyme's kinetic parameters (Km, kcat, kcat /Km, specific activity).

· Describe the catalytic mechanisms employed by the most well-characterized enzymes.

· Describe the mechanisms of enzyme regulation.

Reading Resources

  1. Enzyme Kinetics: Catalysis & Control. Author: Daniel L. Purich. Academic Press (2010) ISBN: 978-0-12-380924-7.
  2. Molecular and Cellular Enzymology (Volumes I & II). Authors: Jeannine Yon-Kahn · Guy Herv´. Springer-Verlag Berlin Heidelberg (2010) ISBN 978-2-86883-816-2
  3. Enzymes: A Practical Introduction to Structure, Mechanism, and Data Analysis. Author: Robert A. Copeland. Wiley-VCH (2000) ISBNs: 0-471-35929-7
  4. ENZYMES: Biochemistry, Biotechnology and Clinical Chemistry. Authors: Trevor Palmer and Philip L. Bonner (2007) ISBN: 978-1-904275-27-5.

Course Requirements

There will be partial exams, a comprehensive final exam and short presentations.

 

Previous Courses Offered (2009-2020)

  • The Molecular Basis of Cancer (Ph.D of Biochemistry)
  • Advanced Biochemical Engineering (Ph.D of Biotechnology)
  • Cell signaling (Ph.D of Biochemistry)
  • Protein Stability and Folding (M.Sc of Biochemistry)
  • Protein Structure (M.Sc of Biochemistry)
  • Advanced Topics in Biochemistry (Ph.D of Biochemistry)
  • Enzymology (M.Sc of Biochemistry)
  • Biophysical Chemistry (M.Sc of Biochemistry)
  • Basic Biochemistry (B.Sc of Cell and Molecular Biology)
  • Plant Biochemistry (M.Sc of Plant Physiology and Ph.D of Gardening)

 

Editorial Board Member.

Iranian Journal of Science and Technology, Transactions A: Science (SpringerNature)

 

Collaborations

  1. Binding and crystallography studies on the complexes of a novel antagonistic peptide of VEGF-A/VEGF-B with Domain 2 of Vascular Endothelial Growth Factor Receptor-1 and Domain 2 and 3 of Vascular Endothelial Growth Factor Receptor-2, The European association for cancer research (EACR) travel fellowship award (Home supervisor: SM Asghari, Host supervisor: Prof. Matthew R. Groves, University of Groningen) (2019-2020).
  2. In recent years, we have several collaborations with the Preclinical Core Facility of Tehran University of Medical Sciences. This center provides animal-PET, micro-CT and animal-SPECT imaging facilities, which rigorously potentiated our studies in the field of translational research.
  3. In collaboration with Shahid Beheshti University of Medical Sciences Ophthalmic Research Center, we aim to apply our anti-angiogenic peptides for treatment of the neovascular angiogenesis in AMD.
  4. In collaboration with Research Center for Nuclear Medicine, and Department of Radiopharmacy, TUMS, Tehran, and Professor Ameneh Rezayof from College of Science, University of Tehran, we use our VEGFR-binding peptides, e.g. as peptide-DTPA-Gd or peptide-DTPA-Ga68, for contrast enhancement in MRI and PET imaging in breast and brain tumor models.

 

Courses

Enzymology

Enzymology is the branch of biochemistry aiming to understand how enzymes work through the relationship between structure and function and how they fold into their native state. This multidisciplinary research field integrates areas of biochemistry, microbiology, molecular biology, molecular genetics, and biophysics. In addition, given the therapeutic and commercial success of small-molecule enzyme inhibitors, as exemplified by kinase inhibitors in oncology, a major focus of current drug-discovery and development efforts is on enzyme targets.

Syllabus Details

1) Enzyme classification. 2) Oligomeric enzymes (Advantages of enzyme oligomerization). 3) Transition state theory. 4) Explaining the efficiency of enzyme catalysis. 5) Chemical kinetics. 6) Enzyme active site. 7) Kinetics of one-substrate enzymatic reactions. 8) Methods for plotting initial-rate data. 9) Bisubstrate kinetic mechanisms. 10) Factors affecting the activity of enzymes. 11) Enzyme inhibition. 12) Brief fundamentals of enzyme assay. 13) How calculate the enzyme reaction rate, Km, kcat, kcat/Km, and specific activity. 14) Examples of enzyme mechanism.

Student Learning Outcomes

The major learning objective of the course is to understand the thermodynamic basis of catalysis, theories of enzyme kinetics, the mechanisms of enzyme catalysis, enzyme assay and the mechanisms of enzyme regulation in the cell. At the conclusion of the course students should be able to:

· Describe transition-state theory and Arrhenius equation.

· Describe and use the equations of enzyme kinetics.

· Describe the methods used in enzyme kinetics.

· Describe the principles of enzyme inhibition.

· Describe the mechanisms of enzyme catalysis.

· Describe the determination of enzyme's kinetic parameters (Km, kcat, kcat /Km, specific activity).

· Describe the catalytic mechanisms employed by the most well-characterized enzymes.

· Describe the mechanisms of enzyme regulation.

Reading Resources

  1. Enzyme Kinetics: Catalysis & Control. Author: Daniel L. Purich. Academic Press (2010) ISBN: 978-0-12-380924-7.
  2. Molecular and Cellular Enzymology (Volumes I & II). Authors: Jeannine Yon-Kahn · Guy Herv´. Springer-Verlag Berlin Heidelberg (2010) ISBN 978-2-86883-816-2
  3. Enzymes: A Practical Introduction to Structure, Mechanism, and Data Analysis. Author: Robert A. Copeland. Wiley-VCH (2000) ISBNs: 0-471-35929-7
  4. ENZYMES: Biochemistry, Biotechnology and Clinical Chemistry. Authors: Trevor Palmer and Philip L. Bonner (2007) ISBN: 978-1-904275-27-5.

Course Requirements

There will be partial exams, a comprehensive final exam and short presentations.

 

Previous Courses Offered (2009-2020)

  • The Molecular Basis of Cancer (Ph.D of Biochemistry)
  • Advanced Biochemical Engineering (Ph.D of Biotechnology)
  • Cell signaling (Ph.D of Biochemistry)
  • Protein Stability and Folding (M.Sc of Biochemistry)
  • Protein Structure (M.Sc of Biochemistry)
  • Advanced Topics in Biochemistry (Ph.D of Biochemistry)
  • Enzymology (M.Sc of Biochemistry)
  • Biophysical Chemistry (M.Sc of Biochemistry)
  • Basic Biochemistry (B.Sc of Cell and Molecular Biology)
  • Plant Biochemistry (M.Sc of Plant Physiology and Ph.D of Gardening)