TOTT is an amino acid derivative used as a chemically modified building block in peptide and bioconjugation workflows. The molecule bears amino and carboxyl functionality characteristic of amino acid frameworks while incorporating an additional substituent pattern implied by the derivative designation, which modulates side-chain reactivity and chemoselectivity during coupling or functionalization. In synthetic chemistry contexts, TOTT is employed to introduce a defined amino-acid-based handle into larger peptide-related intermediates or to support structure-activity studies and analytical method development where controlled variation of amino acid side-chain features is required.
CAT No: CP26891
CAS No:255825-38-8
Synonyms/Alias:2-(1-Oxy-pyridin-2-yl)-1,1,3,3-tetramethylisothiouronium tetrafluoroborate;TOTT (S-(1-Oxido-2-pyridyl)-N,N,N′,N′-tetramethylthiouronium tetrafluoroborate)
TOTT is a specialized amino acid-derived reagent supplied for research workflows that require a defined, amino-acid-like scaffold and controlled reactivity rather than direct use as a proteinogenic building block. In practice, TOTT is selected when downstream synthesis or labeling steps benefit from a stable, pre-organized functionalized format that can be carried through peptide, conjugation, or analytical preparation workflows with consistent handling. Researchers typically choose TOTT to streamline reagent sourcing for custom molecular construction where the reagent's built-in functionality is the key determinant of performance.
1. Peptide-Related Intermediate Use
TOTT is used in peptide chemistry as a defined amino-acid-derived intermediate for assembling custom peptide segments and related peptide building blocks. Teams performing custom peptide synthesis and medicinal chemistry often rely on such reagents to standardize inputs for downstream coupling and purification workflows, especially when the reagent's functionalized format improves reproducibility during intermediate preparation. This application is particularly relevant in contractor-led peptide manufacturing and internal peptide development where consistent reagent identity and reactivity reduce batch-to-batch variability.
2. Chemical Biology Conjugation Workflows
TOTT is applied in chemical biology projects that require controlled incorporation of an amino-acid-like unit into larger molecular constructs, including conjugates used for binding studies, reagent development, and workflow-specific labeling. Research groups in chemical biology and bioconjugation commonly select amino-acid-derived reagents when they want a predictable scaffold that can be carried through multi-step assembly toward a final probe, tag, or modified biomolecule. In these settings, TOTT functions as a practical upstream input that supports reliable downstream functionalization and analytical verification.
3. Analytical Standard Preparation
TOTT is also used for analytical method development and reference material preparation in laboratories that need a defined compound for instrument qualification, chromatographic behavior tracking, or mass spectrometric confirmation. Analytical chemistry teams often select amino-acid-derived reagents like TOTT when they require a stable, well-characterized input that matches the chemical features of target analytes or intermediates used in their workflows. This use case is common in LC-MS and related characterization pipelines for confirming identity, monitoring derivatization steps, and supporting method transfer between systems or laboratories.
4. Pharmaceutical Intermediate Development
TOTT is frequently positioned in pharmaceutical intermediate development programs where a consistent, amino-acid-derived scaffold is needed to build more complex structures for medicinal chemistry campaigns. Process development and synthetic chemistry teams use such intermediates to de-risk downstream assembly by locking in a defined reagent form early in the route. In these workflows, TOTT is valued as a practical procurement-grade building block that supports scalable intermediate handling and downstream transformation toward candidate-relevant structures.
2. High fat diet and GLP-1 drugs induce pancreatic injury in mice
4. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
5. The spatiotemporal control of signalling and trafficking of the GLP-1R
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