763139-35-1

Basic information

• Product Name: Boc-δ-azido-Nva-OH · DCHA
• Synonyms: Boc-δ-azido-Nva-OH · DCHA;Boc-d-azido-Nva-OH · DCHA;Boc-Orn(N2)-OH;Boc-L-Orn(N3)-OH*CHA;5-Azido-N-Boc-L-Norvaline;(S)-Boc-2-amino-5-azido-pentanoic acid cyclohexylamine salt;Boc-Orn(N3)-OH·CHA;Nα-Boc-Nδ-Azido-L-Ornithine cyclohexylammonium salt>98%
• CAS NO: 763139-35-1
• Molecular Formula: C₁₀H₁₈N₄O₄
• Molecular Weight: 258.27432
• Mol File: 763139-35-1.mol
• Article Data: 7

Chemical Properties

• Appearance: /
• CAS DataBase Reference: Boc-δ-azido-Nva-OH · DCHA(CAS DataBase Reference)
• NIST Chemistry Reference: Boc-δ-azido-Nva-OH · DCHA(763139-35-1)
• EPA Substance Registry System: Boc-δ-azido-Nva-OH · DCHA(763139-35-1)

Safety Data

• Hazardous Substances Data: 763139-35-1(Hazardous Substances Data)

Usage

General Description

Boc-δ-azido-Nva-OH · DCHA is a chemical compound with the molecular formula C25H46N6O4. It is a derivative of Boc-δ-azido-Nva-OH, which is a protected form of the amino acid (2S, 4S)-4-amino-2-(1H-1,2,3-triazol-4-yl)butanoic acid. The compound is commonly used in organic synthesis as a building block for the preparation of peptide libraries and combinatorial chemistry. The presence of the Boc (tert-butyloxycarbonyl) protecting group and the azido functionality make it a versatile precursor for the development of new peptide-based drugs and materials. Furthermore, the addition of the DCHA (1,8-diazabicyclo[5.4.0]undec-7-ene) base helps to facilitate various reactions in the synthesis process. Overall, Boc-δ-azido-Nva-OH · DCHA is a valuable compound in the field of peptide chemistry and drug discovery.

Upstream product

• 24424-99-5 di-tert-butyl dicarbonate 
• 2480-93-5 Boc-Orn(Z)-OH 
• 21887-64-9 N₂-(tert-butoxycarbonyl)-L-ornithine 

Downstream Products

• 1224702-11-7 (S)-benzyl 5-azido-2-(tert-butoxycarbonylamino)pentanoate 
• 1310039-64-5 C₃₁H₄₉N₇O₆Si 
• 156463-09-1 2-amino-5-azidopentanoic acid 

Relevant articles and documents

Peptides

A peptide which can adopt a 310-helical conformation in which the side chains of two amino acid residues in the peptide backbone are linked by a group comprising an aromatic 5-membered ring.

A diversity-oriented synthesis strategy enabling the combinatorial-type variation of macrocyclic peptidomimetic scaffolds

Macrocyclic peptidomimetics are associated with a broad range of biological activities. However, despite such potentially valuable properties, the macrocyclic peptidomimetic structural class is generally considered as being poorly explored within drug discovery. This has been attributed to the lack of general methods for producing collections of macrocyclic peptidomimetics with high levels of structural, and thus shape, diversity. In particular, there is a lack of scaffold diversity in current macrocyclic peptidomimetic libraries; indeed, the efficient construction of diverse molecular scaffolds presents a formidable general challenge to the synthetic chemist. Herein we describe a new, advanced strategy for the diversity-oriented synthesis (DOS) of macrocyclic peptidomimetics that enables the combinatorial variation of molecular scaffolds (core macrocyclic ring architectures). The generality and robustness of this DOS strategy is demonstrated by the step-efficient synthesis of a structurally diverse library of over 200 macrocyclic peptidomimetic compounds, each based around a distinct molecular scaffold and isolated in milligram quantities, from readily available building-blocks. To the best of our knowledge this represents an unprecedented level of scaffold diversity in a synthetically derived library of macrocyclic peptidomimetics. Cheminformatic analysis indicated that the library compounds access regions of chemical space that are distinct from those addressed by top-selling brand-name drugs and macrocyclic natural products, illustrating the value of our DOS approach to sample regions of chemical space underexploited in current drug discovery efforts. An analysis of three-dimensional molecular shapes illustrated that the DOS library has a relatively high level of shape diversity.

Stapling of a 310-helix with click chemistry

Short peptides are important as lead compounds and molecular probes in drug discovery and chemical biology, but their well-known drawbacks, such as high conformational flexibility, protease lability, poor bioavailability and short half-lives in vivo, have prevented their potential from being fully realized. Side chain-to-side chain cyclization, e.g., by ring-closing olefin metathesis, known as stapling, is one approach to increase the biological activity of short peptides that has shown promise when applied to 310-and α-helical peptides. However, atomic resolution structural information on the effect of side chain-to-side chain cyclization in 310-helical peptides is scarce, and reported data suggest that there is significant potential for improvement of existing methodologies. Here, we report a novel stapling methodology for 310-helical peptides using the copper(I)-catalyzed azide-alkyne cycloaddition (CuAAC) reaction in a model aminoisobutyric acid (Aib) rich peptide and examine the structural effect of side chain-to-side chain cyclization by NMR, X-ray diffraction, linear IR and femtosecond 2D IR spectroscopy. Our data show that the resulting cyclic peptide represents a more ideal 310-helix than its acyclic precursor and other stapled 310-helical peptides reported to date. Side chain-to-side chain stapling by CuAAC should prove useful when applied to 3 10-helical peptides and protein segments of interest in biomedicine.(Figure Presented)