Oktay Kazim Gasymov

Place of birth

Zakatala district, Azerbaijan Republic

Date of birth

04 August 1958

Education

Azerbaijan (now Baku) State University, Faculty of Physics

Scientific degree

Dr.Sci

Academic rank

Professor

Speciality code and title for PhD thesis

2206.01 — Molecular Physics

Speciality code and title for doctoral thesis

2406.02 -  Biophysics

2415.01- Ecology

Free radical processes in proteins during mechanical destruction

Date of Election as a Corresponding Member and speciality

02 May 2017,  Biophysics

Total number of printed scientific publications

126

Number of scientific publications printed abroad

117

Number of papers published in journals indexed and abstracted in international databases

Number of patents and certificates of authorship

3

Staff training:

-          number of PhD

-          number of Doctor of sciences

2

Key scientific achievements

1.    The initial free-radical processes occurring during the mechanical degradation of proteins, as well as the chain photo- and thermoreactions of these radicals, were determined. It was shown that during mechanical degradation of proteins, only one of the three covalent bonds in the polypeptide chain—specifically the Cα–C bond—undergoes homolytic cleavage (1982–1996).

2.             A new method, “Site-Directed Tryptophan Fluorescence” (SDTF) was developed for determining the three-dimensional solution structure of proteins (1997, 2001).

3.           Evidence was provided that lipids on the surface of the human cornea are removed by the tear lipocalin protein (1999, 2005).

4.           Using the SDTF method, the 3D solution structure of tear lipocalin (2001) was  determined and later confirmed by X-ray crystallographic analysis of the protein crystal (2005).

5.          Using SDTF and Site-Directed Spin Labeling methods, the ligand-binding mechanism of tear lipocalin, including ligand orientation, dynamics, and distribution within the protein cavity  were demonstrated (2000–2010).

6.           Using SDTF, the mechanism of pH-dependent conformational changes in tear lipocalin  was revealed and it was showed that ligand binding is controlled by the protonation state of the Glu27 residue located in the AB loop. This was later confirmed by X-ray structural analysis of the ligand-bound protein (2010).

7.           It was demonstrated that the conserved disulfide bond in the lipocalin family modulates ligand-binding properties (2011).

8.           A new method, “Site-Directed Circular Dichroism” was developed for studying conformational changes in proteins and demonstrated the advantages of low-temperature measurements (2008, 2014).

9.          “Cation–π” interactions in lipocalin family proteins were analyzed and they were characterized in terms of structure–function relationships (2012).

10.       A direct, model-independent method for studying protein–ligand interactions using fluorescence was proposed (2014).

11.       The “double tryptophan exciton” method to evaluate nearby side chains in proteins was  proposed and its capabilities  were demonstrated using tear lipocalin as an example (2015).

12.       Whole human blood and plasma were investigated using surface-enhanced (plasmonic) Raman spectroscopy. Resonance enhancement was observed, and the amplification properties of spectral bands were demonstrated. The potential of this system as a diagnostic tool for various diseases was  showed (2015–2016).

13.       The preparation of silk fibroin films doped with dyes was described. These films preserve the optical properties of monomeric dyes in the solid state, which is important for optical and biolaser applications. FTIR, CD, and XRD analyses of Rhodamine 6G-doped silk fibroin films revealed protein secondary structure and interactions with the dye. UV–Vis and exciton CD spectra explained the structure of Rhodamine and showed that the silk fibroin environment prevents dimer formation. These films are promising for innovative photonic technologies.

14.       It was demonstrated that ANS fluorescence is an effective method for studying protein structure in the solid state. Studies on silk fibroin from Bombyx mori showed that ANS binds to different hydrophobic regions with varying water interactions. The method is applicable to studying protein aggregates and amyloids, including those associated with Alzheimer’s, Parkinson’s, and prion diseases.

15.       For early diagnosis of lung cancer, a model based on FTIR spectra and artificial intelligence algorithms (Linear SVM, PLS-DA, Random Forest) was used to analyze blood plasma samples from healthy individuals and patients. The method achieved 80–90% accuracy and can serve as a rapid, minimally invasive, and cost-effective screening tool (2021).

16.      Age-related neurodegenerative diseases (e.g., Alzheimer’s and Parkinson’s) are mainly caused by abnormal accumulation of beta-amyloid and other proteins, oxidative stress, and progressive neuronal damage. The study showed that fusidic acid not only inhibits beta-amyloid formation but also promotes the degradation of existing amyloids, suggesting potential therapeutic applications beyond its antibiotic use (2021).

17.       Molecular docking studies showed that the cationic pentapeptide Glu–Gln–Arg–Pro–Arg and its D-isomers are multifunctional and may exhibit activity against both cancer and COVID-19. Their activity is related to binding to integrins (α5β1 and αIIbβ3), viral Mpro and S proteins, and the ACE2 receptor. D-isomer modification allows functional tuning, suggesting potential therapeutic applications (2021).

18.       In silico docking studies showed that the Glu–Gln–Arg–Pro–Arg pentapeptide directly interacts with and inhibits cancer-related EGFR and FYN proteins. Binding affinities and ADME analysis indicate high pharmacological potential, suggesting its promise for lung cancer treatment (2023).

19.       Neutral, positively charged, and hydrophobic spin probes were studied to distinguish healthy and cancer cell membranes. Results showed that hydrophobic TEMPO-benzoate penetrates cancer cell liposomes more effectively, while positively charged 4-amino-TEMPO does not penetrate either type. This indicates TEMPO-benzoate is a better probe and may be useful for targeted drug delivery (2023).

20.       Personalized drug dosing and treatment duration are essential for improving efficacy and reducing side effects. A highly sensitive biosensor was developed to measure doxorubicin (DOX) concentration in plasma: a classical LSPR-based sensor detected nanomolar levels, while a new Au/Al₂O₃ nano-island sensor achieved picomolar sensitivity (2024).

21.       Lipid structural properties in cancer cell membranes differ significantly from healthy cells, with transitions occurring at lower temperatures and in a non-cooperative manner. Interestingly, some morphologically normal cells exhibited lipid behavior similar to cancer cells, suggesting that metabolic changes may precede morphological alterations and that morphology alone may be insufficient for diagnosis (2025).

Titles of publications

1. Gasymov O.K., Abduragimov A.R., Yusifov T.N., Glasgow B.J. Structural changes in human tear lipocalins associated with lipid binding. Biochim.Biophys.Acta, 1998; 1386(1); 145-156.

2. Gasymov O.K., Abduragimov A.R., Yusifov T.N., Glasgow B.J. Resolution of ligand positions by site directed tryptophan fluorescence in tear lipocalin. Protein Science, 2000, 9, 2, 337-343.

3. Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. Site Directed Tryptophan Fluorescence Reveals the Solution Structure of Tear Lipocalin: Evidence for features that confer promiscuity in ligand binding, Biochemistry, 2001, 40, 14754-14762.

4. Gasymov OK, Abduragimov AR, Prasher P, Yusifov TN and Glasgow BJ. Tear Lipocalin: Evidence for a Scavenging Function to Remove Lipids from the Human Corneal Surface. Invest Ophthalmol Vis Sci., 2005, 43(10), 3165-73.

5. Gasymov OK, Abduragimov AR, Glasgow BG. Intracavitary Ligand Distribution in Tear Lipocalin by Site-Directed Tryptophan Fluorescence, Biochemistry, 2009, 48 (30) 7219-7228.

6. Gasymov OK, Abduragimov AR, Glasgow BG. PH-dependent Conformational Changes in Tear Lipocalin by Site Directed Tryptophan Fluorescence, Biochemistry, 2010, 49 (3), 582-590.

7. Gasymov OK, Abduragimov AR, Glasgow BG. Excited Protein States of Human Tear Lipocalin for Low- and High-Affinity Ligand Binding Revealed by Functional AB Loop Motion, Biophysical Chem, 2010, 149(1-2), 47-57.

8. Gasymov OK, Abduragimov AR, Glasgow BG. Cation-π Interactions in Lipocalins: Structural and Functional Implications, Biochemistry, accelerated publication, 2012, 51(14), 2991-3002.

9. Gasymov OK, Abduragimov AR, Glasgow BG. Double Tryptophan Exciton Probe to Gauge Proximal Side Chains in Proteins- Augmentation at Low Temperature, J Phys Chem B., 2015, 119(10), 3962-3968.

10. Gasymov OK, Alekperov OZ, Aydemirova AH, Kamilova N, Aslanov RB, Bayramov AH, Kerimova A,  Surface enhanced Raman scattering of whole human blood on nano-structured ZnO surface, Phys. Status Solidi C, 2017, 1600155

11. Ragona L., Gasymov O.K., Guliyeva A.J., Aslanov R.B., Zanzoni S., Botta Ch., Molinari H., Rhodamine binds to silk fibroin and inhibits its self-aggregation, BBA-Proteins and Proteomics, 2018, 1866, 661-667.

12. Aslanov RB, Dashdemirova LM, Alekperov OZ, Abdurahimov AR, Gasymov OK, Dynamics of Proteins by Thermal Decay of Free Radicals Induced by Ultraviolet Irradiation, Journal of Spectroscopy, 2018, v. 2018, ID 6197636.

13. Aydemirova A.H., Kamilova N., Gasymov OK., FTIR of human blood plasma as a diagnostic tool for myoma patients, International Scientific Conference "Molecular, Membrane and Cellular Basics of Biosystems Operation", Minsk, Belarus, 27-29 June 2018, p.184

14.  Gasymov OK, Botta Ch, Ragona L, Guliyeva AJ, Molinari H, Silk fibroin-based films enhance rhodamine 6G emission in the solid state: A chemical-physical analysis of their interactions for the design of highly emissive biomaterials, Macromol.Chem.Phys, 2019, v 220, 1800460.

15. Guliyeva A.J., Gasymov OK. ANS fluorescence: potential to characterize proteins in solid states, Biochemical and Biophysical reports, 2020, 24, 100843.

16. Gasanova R.B.,  Melikova L.A.,  Gasymov O.K.,  Aliyev J.A., Zeta potentials of healthy and cancer cells of human lung: implication to cancer therapy, The Modern Achievements of Azerbaijan Medicine, 2020, 4, 112-117.

17. Gasymov OK, Aydemirova A., Melikova L, Aliyev JA, Artificial Intelligence to Classify Human Lung Carcinoma Using Blood Plasma FTIR Spectra, Applied and Computational Mathematics, 2021, 20, 277-289. (IF= 3.898)

18. Gasymov OK, Celik S, Agaeva G, Akyuz S, Kecel-Gunduz S, Qocayev NM, Ozel AE, Agaeva U, Bakhishova M, Aliyev JA, Cationic pentapeptide, GLU-GLN-ARG-PRO-ARG, and its D-isomer analogs: theoretical and structural studies for potential anti-cancer and novel anti-COVID-19 applications, 4^th International New York Conference on Evolving Trends in Interdisciplinary Research and Practices, Oral Presentation, May 2-4, 2021, Abstract Book, 28-29, Manhattan, New York City.

19. Gasymov OK, Celik S, Agaeva G, Akyuz S, Kecel-Gunduz S, Qocayev NM, Ozel AE, Agaeva U, Bakhishova M, Aliyev JA, Evaluation of anti-cancer and anti-Covid-19 properties of cationic pentapeptide Glu-Gln-Arg-Pro-Arg,  from Rice Bran protein and its D-isomer analogs through molecular docking simulations, Journal Mol Graphics and Modeling, 2021, 108, 107999. (IF= 2.518)

20. Gasymov OK, Mammedzade AM, Bakhishova MJ , Guliyeva AJ, Ragona L, Molinari M, Sodium Fusidate Prevents Protein Aggregation of Silk Fibroin and offers new perspectives for human lens material disaggregation, Biophysical chemistry, 2021, 279, 106680 (IF= 2.352).  

21. M. Bakhishova, S. Celik, S. Kecel-Gunduzb, S. Akyuz, A. E. Ozel, G. Agaeva, L.M.

Suleymanova, U. Agaevad, O.K. Gasymov, J.A. Aliyev., The effect of pentapeptide EQRPR derived from rice bran on the DPPC monolayer, International Korkut Ata Scientific Researches Conference, Osmaniye, Turkey, June 28-30, 2022, Abstracts book, p. 389-390.

22.  Gasymov O.K., Bakhishova M.J., Gasanova R.B., Aslanov R.B., Melikova L.A., Aliyev J.A.,  Benzoate group attachment to TEMPO provides enhanced discrimination of liposomes fabricated using human lung normal and carcinoma cells, Russ.J.Biol.Phys.Chem.,  2022, 7 (2), 261-267.

23. Gasymov O.K., Bakhishova M.J., Gasanova R.B., Aslanov R.B., Melikova L.A., Aliyev J.A. Benzoate group attachment to TEMPO provides enhanced discrimination of liposomes fabricated using human lung normal and carcinoma cells, Proceeding BBPC-2022, Medical Biophysics and Biophysical Chemistry, 126-127.

24. Mammedzade A.M., Mammadova Ay.J., Gasymov O.K., Structure of silk fibroin nanoparticles: characterization of hydrophobic patches, Russ.J.Biol.Phys.Chem.,  2022, 7 (2), 268-272.

25. Mammedzade A.M., Mammadova Ay.J., Gasymov O.K., Structure of silk fibroin nanoparticles: characterization of hydrophobic patches, Proceeding BBPC-2022, Medical Biophysics and Biophysical Chemistry, 152-153.

26. Kamilova N.M., Gasymov O.K., Alieva U.G., Comparative Assessment of Hormonal, Echographic and Spectral Parameters in Chronic Endometritis and Chronic Salpingo-Oophoritis, Ukr.J. Med., Biol. Sport, 2022, 7, 143-146.

27. K. Pagano, S. Tomaselli, L. De Rosa, L. D’Andrea, A. M. Mammedzade, O. K. Gasymov, H. Molinari, L. Ragona, Silk Fibroin: Exploring a functional amyloid to investigate aggregation modulators and cross seeding effects, Italian-French International Conference on Magnetic Resonance, 27-30 September, 2022, Milan, Book of Abstract, P-99.

28.  Bakhishova M., Aslanov R.B., Gasanova R.B., Melikova L., Aliyev J.A., Gasymov O.K. Hydrophobic but not charged group attachment to TEMPO enhances discrimination of liposomes from human lung normal and carcinoma cells, Transactions of ANAS (Physics and Astronomy Series), 2022, XLII (5), 56-63.

29. Oktay K. Gasymov, Serda Kecel-Gunduz, Sefa Celik, Sevim Akyüz,  Ayşen E. Ozel, Gulshen Agaeva, Leman M. Suleymanova, Ulker Agaeva, Matanat Bakhishova, J.A. Aliyev, Molecular docking of the pentapeptide derived from rice bran protein as anticancer agent inhibiting both receptor and non-receptor tyrosine kinases, J. Biomol. Struct. Dyn., 2023, 41(10), 4321-4343, doi: 10.1080/07391102.2022.2067234.

30. A.H. Aydəmirova, L.Ə. Məlikova, O.K. Qasımov; Furye Çevirici İnfraqırmızı spektroskopiyanın tətbiqi ilə insanın sağlam və ağciyər adenokarsinoması halında plazma-lipid modelinin diaqnostik mümkünlüyü; Azerbaijan Journal of Physics, Fizika, 2023,v. 29; Section1; pp.3-9

31. Gasymov O.K., Abdurahimov A.R., Development of occupational ophthalmology: from dry eye syndrome to artificial tears, Journal of Life Sciences & Biomedicine, 2023, 5, 50-55.

32. Gasymov O. K., Bakhishova M. J., Aslanov R. B., Melikova L.A., Aliyev J. A., Membrane partitioning of TEMPO discriminates human lung cancer from neighboring normal cells, Acta Naturae, 2023, 15, 111-119 (IF: 2.0 (WOS); 3.5 (Scopus)).

33. Quarta A., Bettini S, Cuscuna M., Lorenzo D., Epifani G., Gigli G., Valli L., Aliyev J.A., Kazimov E.E., Bakhishova M.J., Gasymov O.K., Simone D., Tailoring gold nanoisland-based biosensor for ultrasensitive detection of doxorubicin in biological fluids, ACS Appl. Nano Materials, 2024, 7, 18724-18736 (Q1, IF: 5.3

34. I. Abbasov, M. Musayev, O. Gasymov, J. Huseynov, C. Naziyev, D. Askerov, S. Asadullayeva, N. Ismayilova, A. Mammadova, N. Hashimova, E. Eminova, Influence of background impurities of oxygen and copper on the luminescence spectrum of polycrystalline CVD ZnSe with excess selenium, Nano, 2025, 2550010, IF= 1.0, Cite Score= 2.1, doi: 10.1142/S1793292025500109

35. V. Atayeva, O. Gasymov, A. Salmanova, Physiological and Biological Potential of Dark-Red Autumn Leaves of Smilax Excelsa L., Journal of Food Science and Technology (Iran) (JFST), 2025, 22, 51-61.

36. O.K. Gasymov, M. J. Bakhishova, L. Melikova, J.A. Aliyev, Structural organizations of membrane lipids from human lung cancer and healthy cell, Journal of Molecular Structure, 2025, 1350, 144133, IF= 4.7

Membership in national, international, and foreign scientific organizations

Pedagogical activity

2001–2012 — University of California, Los Angeles (UCLA)

2016–present — Azerbaijan National Academy of Sciences (ANAS), Master’s training

Other activities

Member of editorial boards of scientific journals

Awards and prizes

1.  Jubilee Medal of the 100th Anniversary of Baku State University (1919–2019)

2.  Jubilee Medal of the 100th Anniversary of Azerbaijan State Pedagogical University (1921–2021)

3.  “Labor” Order, 3rd Class

Place of work and its address

Institute of Molecular Biology, (Public Legal Entity), AZ1073, 11 Izzat Nabiyev Street, Baku, Azerbaijan

Position

Head of Laboratory

Office phone

432-6248

Mobile

(055) 533-6648

Home

Fax

E-mail

oktaygasimov@gmail.com