Ali Akbar Saboury

University of Tehran

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Co-Authors

Ali Akbar Moosavi‐Movahedi

University of Tehran

167

Adeleh Divsalar

Kharazmi University

130

G. Rezaei Behbehani

Imam Khomeini International University

Thomas Haertlé

University of Tehran

Hassan Mansouri‐Torshizi

University of Sistan and Baluchestan

Faizan Ahmad

Universidade Federal de Viçosa

Mohammad Reza Ganjali

Mashhad University of Medical Sciences

Behzad Shareghi

Shahrekord University

Mojtaba Falahati

Erasmus MC

G. H. HAKIMELAHI

Institute of Chemistry, Academia Sinica

Cooperative Institutions

University of Tehran

428

Tehran University of Medical Sciences

134

Tarbiat Modares University

Islamic Azad University, Tehran

Shiraz University

Hannah Research Foundation

Islamic Azad University, Science and Research Branch

Payame Noor University

Shahid Beheshti University

Shahid Beheshti University of Medical Sciences

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Tau folding and cytotoxicity of neuroblastoma cells in the presence of manganese oxide nanoparticles: Biophysical, molecular dynamics, cellular, and molecular studies

International Journal of Biological Macromolecules (2018)

Parvaneh Mehdizadeh Samaneh Sadat Hashemi Fesharaki Mina Nouri Mahsa Ale‐Ebrahim Keivan Akhtari

Viability assay

SH-SY5Y

Docking (animal)

10.1016/j.ijbiomac.2018.11.191

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Citations (17)

A High Performance Theory for Thermodynamic Study on the Binding of Human Serum Albumin with Erbium Chloride

Chinese Journal of Chemistry (2009)

G. Rezaei Behbehani Adeleh Divsalar Ali Akbar Saboury Farnoush Faridbod Mohammad Reza Ganjali

Abstract A thermodynamic study of the interaction between erbium(III) chloride (Er 3+ ) and human serum albumin (HSA) was studied at pH=7.0, 27 and 37 °C in phosphate buffer by isothermal titration calorimetry (ITC). The present study reports the thermodynamic parameters that govern HSA‐Er 3+ interactions. The extended solvation theory was used to reproduce the enthalpies of HSA‐Er 3+ interactions over the whole range of Er 3+ concentrations. The binding parameters recovered from the new model were attributed to the structural change of HSA and its biological activity. The results obtained indicate that there is a set of two identical binding sites for Er 3+ ions with negative cooperativity. The enhancement of complex formation by Er 3+ and concomitant increase in ? S suggest that the metal ion plays a role in increasing the number of hydrophobic contacts. The binding parameters discovered from the extended solvation model indicate that the stability of HSA molecule is increased as a result of its interaction with Er 3+ ions.

Isothermal Titration Calorimetry

Human serum albumin

Cooperativity

Hydrophobic effect

Cooperative binding

10.1002/cjoc.200990046

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Citations (6)

Reactive oxygen species generated by titanium oxide nanoparticles stimulate the hemoglobin denaturation and cytotoxicity against human lymphocyte cell

Journal of Biomolecular Structure and Dynamics (2019)

Fakhteh Aliakbari Sara Haji Hosseinali Ziba Khalili Sarokhalil Koorosh Shahpasand Ali Akbar Saboury

With the development of nanomaterials, there has been an enormous interest in the medical, biotechnological and chemical applications of nanoparticles (NPs). They are widely used for cancer therapy...

Nanomaterials

Denaturation (fissile materials)

Titanium oxide

Nanotoxicology

10.1080/07391102.2019.1568305

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Citations (17)

Inhibition of HEWL fibril formation by taxifolin: Mechanism of action

PLoS ONE (2017)

Mohsen Mahdavimehr Ali Akbar Meratan Maryam Ghobeh Atiyeh Ghasemi Ali Akbar Saboury

Among therapeutic approaches for amyloid-related diseases, attention has recently turned to the use of natural products as effective anti-aggregation compounds. Although a wealth of in vitro and in vivo evidence indicates some common inhibitory activity of these compounds, they don't generally suggest the same mechanism of action. Here, we show that taxifolin, a ubiquitous bioactive constituent of foods and herbs, inhibits formation of HEWL amyloid fibrils and their related toxicity by causing formation of very large globular, chain-like aggregates. A range of amyloid-specific techniques were employed to characterize this process. We found that taxifolin exerts its effect by binding to HEWL prefibrillar species, rather than by stabilizing the molecule in its native-like state. Furthermore, it's binding results in diverting the amyloid pathway toward formation of very large globular, chain-like aggregates with low β-sheet content and reduced solvent-exposed hydrophobic patches. ThT fluorescence measurements show that the binding capacity of taxifolin is significantly reduced, upon generation of large protofibrillar aggregates at the end of growth phase. We believe these results may help design promising inhibitors of protein aggregation for amyloid-related diseases.

Taxifolin

Amyloid (mycology)

Globular protein

Mechanism of Action

10.1371/journal.pone.0187841

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Citations (46)

Involvement of planned cell death of necroptosis in cancer treatment by nanomaterials: Recent advances and future perspectives

Journal of Controlled Release (2019)

Majid Sharifi Sara Haji Hosseinali Ali Akbar Saboury Éva Szegezdi Mojtaba Falahati

Nanotoxicology

10.1016/j.jconrel.2019.02.007