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Peyman Salehi

Researcher at Shahid Beheshti University

Publications -  317
Citations -  6863

Peyman Salehi is an academic researcher from Shahid Beheshti University. The author has contributed to research in topics: Catalysis & Essential oil. The author has an hindex of 41, co-authored 309 publications receiving 6112 citations. Previous affiliations of Peyman Salehi include University of Gilan & University of Isfahan.

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Oxidation of alcohols using (NH4)2Cr2O4 in the presence of Al(HSO4)3 and wet SiO2

TL;DR: In this paper, a mild and efficient method for the oxidation of alcohols by ammonium dichromate in the presence of Al(HSO4)3 and wet SiO2 in solution or under solvent-free conditions is reported.
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Synthesis, antibacterial and antioxidant activity of novel 2,3-dihydroquinazolin-4(1H)-one derivatives of dehydroabietylamine diterpene

TL;DR: A series of 2,3-dihydroquinazolin-4(1H)-ones was synthesized by a three-component reaction between dehydroabietylamine (DHA) diterpene, isatoic anhydride and different aromatic aldehydes in the presence of a catalytic amount of p-toluenesulfonic acid (13 mol%).
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Silica Sulfuric Acid: An Efficient and Reusable Catalyst for the One-Pot Synthesis of 3,4-Dihydropyrimidin-2(1H)-ones.

TL;DR: Silica sulfuric acid as discussed by the authors can be used to catalyse the Biginelli reaction between an aldehyde, a β-dicarbonyl compound and urea or thiourea in refluxing ethanol.
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Hydrodistillation–Headspace Solvent Microextraction: An Efficient Method for Analysis of the Essential Oil from the Seeds of Foeniculum vulgare Mill.

TL;DR: In this article, the effect on extraction efficiency of different conditions, for example sample mass, extraction time, microdrop volume, and choice of solvent, was studied and all were optimized.
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Novel noscapine derivatives stabilize the native state of insulin against fibrillation

TL;DR: It is demonstrated that compounds which stabilize the folded native state of a protein can not only inhibit fibrillation but also decrease the toxicity of the mature fibrillar aggregates of insulin protein.