Publications by authors named "M Hajimahmoodi"

A novel series of 4-nitrophenylpiperazine derivatives (4a-m) was designed and synthesized as potential tyrosinase inhibitors. Comprehensive characterization using H-NMR, C-NMR, CNH, and IR techniques was performed for all target compounds. Subsequently, the derivatives were evaluated for their inhibitory activity against tyrosinase.

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In the category of sports supplements, whey protein powder is one of the popular supplements for muscle building applications. Therefore, verification of the sport supplements as authentic products has become a universal concern. This work aimed to propose vibrational spectroscopy including near infrared (NIR) and infrared (IR) as rapid and non-destructive testing tools for the detection and quantification of maltodextrin, milk powder and milk whey powder in whey protein supplements.

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Due to the lack of pharmacopeia guidelines for injectable microspheres based on poly (D, L-lactide-co-glycolide) (PLGA), an internal method validation is a critical prerequisite for quality assurance. One of the essential issues of developing peptide-based drugs loaded PLGA microspheres is the precise determination of the amount of peptide drug entrapped in the microspheres. The aim of this study is the development and optimization of a method for measuring the drug content loading of PLGA microspheres using exenatide as a model peptide drug.

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In the present study, a series of aryl-substituted thioqunoline conjugated to thiosemicarbazide were rationally designed and synthesized. The formation of target compounds was confirmed by spectral characterization techniques such as IR, H-NMR, C-NMR, ESI-MS, and elemental analysis. Among the synthesized derivatives, compound 10g bearing para-chlorophenyl moiety was proved to be the most potent tyrosinase inhibitor with an IC value of 25.

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Herein, a straightforward synthetic strategy mediated by Ugi reaction was developed to synthesize novel series of compounds as tyrosinase inhibitors. The structures of all compounds were confirmed by FT-IR, H-NMR, C-NMR, and CHNOS techniques. The tyrosinase inhibitory activities of all synthesized derivatives 5a-m were determined against mushroom tyrosinase and it was found that derivative 5c possesses the best inhibition with an IC  value of 69.

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