Tapi-0 provides a peptide-like scaffold used in enzyme-modulation and protein-interaction studies. Its structural arrangement allows exploration of conformational flexibility and steric requirements. Researchers evaluate solvent-dependent folding and binding behavior. Applications include inhibitor design, structural biochemistry, and mechanistic modeling.
CAT No: R2473
CAS No:163958-73-4
Synonyms/Alias:163958-73-4;TAPI 0;TAPI-0;N-[(2R)-2-[2-(Hydroxyamino)-2-oxoethyl]-4-methyl-1-oxopentyl]-3-(2-naphthalenyl)-L-alanyl-L-alaninamide;N-{(2r)-2-[2-(Hydroxyamino)-2-Oxoethyl]-4-Methylpentanoyl}-3-Naphthalen-2-Yl-L-Alanyl-L-Alaninamide;CHEMBL1234732;(2R)-N-[(2S)-1-[[(2S)-1-amino-1-oxopropan-2-yl]amino]-3-naphthalen-2-yl-1-oxopropan-2-yl]-N'-hydroxy-2-(2-methylpropyl)butanediamide;TNF-alpha Protease Inhibitor-0;NHX;SCHEMBL1847906;GLXC-01795;143457-40-3;NGA95873;BDBM50407514;AKOS032962849;DA-78192;PD080349;HY-118694;Q27463822;110-143-1;
Tapi-0, also known as O-(2-Acetamido-2-deoxy-D-glucopyranosylidene)amino N-phenylcarbamate, is a synthetic carbohydrate derivative widely recognized for its unique structural features and utility in scientific research. Characterized by its ability to function as a potent and selective inhibitor of O-GlcNAcase (OGA), this compound plays a significant role in glycoscience studies, particularly in the exploration of O-GlcNAcylation processes. Its distinct molecular architecture allows it to interact specifically with target enzymes, making it a valuable tool for dissecting complex biochemical pathways related to protein glycosylation. Researchers appreciate Tapi-0 for its stability and solubility in aqueous environments, which facilitates its use in a range of experimental protocols. Its application extends across several fields, serving as a cornerstone in the investigation of cellular signaling, metabolic regulation, and epigenetic modifications.
Biochemical Pathway Elucidation: In the context of biochemical research, Tapi-0 is extensively utilized to study the dynamic regulation of O-GlcNAcylation, a reversible post-translational modification of intracellular proteins. By selectively inhibiting OGA, the compound allows scientists to increase O-GlcNAc levels on target proteins, thereby enabling the investigation of how this modification influences cellular processes such as signal transduction, transcription, and proteostasis. The use of this inhibitor has provided new insights into the cross-talk between phosphorylation and glycosylation, revealing intricate regulatory networks that control cell fate decisions and stress responses.
Cellular Signaling Studies: Researchers employ O-(2-Acetamido-2-deoxy-D-glucopyranosylidene)amino N-phenylcarbamate to dissect the role of O-GlcNAc cycling in cellular signaling pathways. By modulating the activity of OGA, it becomes possible to observe the downstream effects on key signaling molecules, including kinases and transcription factors. This approach has shed light on the involvement of O-GlcNAcylation in processes such as cell growth, differentiation, and apoptosis, offering a deeper understanding of how cells integrate metabolic cues with signaling networks to maintain homeostasis.
Epigenetic Regulation Research: The influence of O-GlcNAcylation on chromatin structure and gene expression has become a focal point of epigenetic studies. Tapi-0 serves as a critical tool for modulating O-GlcNAc levels on histones and chromatin-associated proteins. Through its application, scientists can probe the relationship between glycosylation events and epigenetic modifications such as methylation and acetylation, thereby elucidating mechanisms underlying transcriptional regulation and genome stability. This capability is particularly valuable for exploring how environmental and metabolic factors impact epigenetic landscapes.
Proteomics and Systems Biology: In proteomics, the use of this OGA inhibitor facilitates the identification and quantification of O-GlcNAc-modified proteins on a global scale. By stabilizing O-GlcNAc marks, researchers can employ advanced mass spectrometry techniques to map glycosylation sites and assess their functional relevance in various biological contexts. This systems-level approach enables the discovery of novel protein substrates, interaction partners, and regulatory motifs, contributing to a comprehensive understanding of cellular complexity.
Neuroscience and Neurodegeneration Studies: The application of Tapi-0 extends into neuroscience, where it is used to investigate the role of O-GlcNAcylation in neuronal function and neurodegenerative processes. By modulating OGA activity in neuronal models, scientists can examine how altered glycosylation patterns affect synaptic plasticity, axonal transport, and protein aggregation. These studies are instrumental in uncovering molecular mechanisms associated with learning, memory, and the progression of neurodegenerative disorders, highlighting the broad research value of this versatile carbohydrate compound.
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