Identification of Novel N-(Aryl)-3-(N-benzylsulfamoyl)benzamides as NAMPT Activators
Fikriye Özgencil(GAZI UNIVERSITY, FACULTY OF PHARMACY, DEPARTMENT OF PROFESSIONAL PHARMACEUTICAL SCIENCES, DEPARTMENT OF PHARMACEUTICAL CHEMISTRY)0000-0003-3664-4150
Gökçen Eren(GAZI UNIVERSITY, FACULTY OF PHARMACY, DEPARTMENT OF PROFESSIONAL PHARMACEUTICAL SCIENCES, DEPARTMENT OF PHARMACEUTICAL CHEMISTRY)0000-0002-3420-607X
In addition, molecular docking studies were conducted within both the catalytic and allosteric sites of NAMPT, and the resulting binding patterns were analyzed to correlate structural differences with the observed in vitro NAMPT activity, highlighting the significance of molecular interactions.
📌 3 Key Takeaways
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Objective & Hypothesis:Nicotinamide adenine dinucleotide (NAD⁺) plays a central role in numerous physiological processes, and maintaining or increasing cellular NAD⁺ levels has emerged as a promising strategy for promoting healthy aging.
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Key Findings & Data:Nicotinamide phosphoribosyltransferase (NAMPT) is the rate-limiting enzyme in the NAD+ salvage pathway, which makes it an attractive target for the treatment of many diseases associated with NAD+ depletion, such as inflammation, neurodegenerative, and metabolic diseases.
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Conclusion & Impact:In addition, molecular docking studies were conducted within both the catalytic and allosteric sites of NAMPT, and the resulting binding patterns were analyzed to correlate structural differences with the observed in vitro NAMPT activity, highlighting the significance of molecular interactions.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:NAMPT · activator · molecular docking
Abstract
Nicotinamide adenine dinucleotide (NAD⁺) plays a central role in numerous physiological processes, and maintaining or increasing cellular NAD⁺ levels has emerged as a promising strategy for promoting healthy aging. Nicotinamide phosphoribosyltransferase (NAMPT) is the rate-limiting enzyme in the NAD+ salvage pathway, which makes it an attractive target for the treatment of many diseases associated with NAD+ depletion, such as inflammation, neurodegenerative, and metabolic diseases. Herein, we report the synthesis and in vitro biological evaluation of STA1-STA3, which increased NAMPT activation by 2- to 38-fold. In addition, molecular docking studies were conducted within both the catalytic and allosteric sites of NAMPT, and the resulting binding patterns were analyzed to correlate structural differences with the observed in vitro NAMPT activity, highlighting the significance of molecular interactions.
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