181760-14-5

Basic information

• Product Name: Carbamic acid, [(1S,2S)-1-ethynyl-2-methylbutyl]-, 1,1-dimethylethyl ester (9CI)
• Synonyms: Carbamic acid, [(1S,2S)-1-ethynyl-2-methylbutyl]-, 1,1-dimethylethyl ester (9CI)
• CAS NO: 181760-14-5
• Molecular Formula: C₁₂H₂₁NO₂
• Molecular Weight: 211.30064
• Product Categories: N-BOC
• Mol File: 181760-14-5.mol

Chemical Properties

• Appearance: /
• CAS DataBase Reference: Carbamic acid, [(1S,2S)-1-ethynyl-2-methylbutyl]-, 1,1-dimethylethyl ester (9CI)(CAS DataBase Reference)
• NIST Chemistry Reference: Carbamic acid, [(1S,2S)-1-ethynyl-2-methylbutyl]-, 1,1-dimethylethyl ester (9CI)(181760-14-5)
• EPA Substance Registry System: Carbamic acid, [(1S,2S)-1-ethynyl-2-methylbutyl]-, 1,1-dimethylethyl ester (9CI)(181760-14-5)

Safety Data

• Hazardous Substances Data: 181760-14-5(Hazardous Substances Data)

Upstream product

• 181760-06-5 [(1S,2S)-1-(2,2-Dibromo-vinyl)-2-methyl-butyl]-carbamic acid tert-butyl ester 
• 118171-79-2 N-(t-butoxycarbonyl)-isoleucine aldehyde 
• 4202-14-6 dimethyl (2-oxopropyl)phosphonate 
• 90965-06-3 dimethyl 1-(1-diazo-2-oxopropyl)phosphonate 
• 27491-70-9 dimethyl diazomethylphosphonate 
• 13139-16-7 N-(tert-butyloxycarbonyl)-L-isoleucine 
• 87694-51-7 N-(tert-butoxycarbonyl)-L-isoleucine N'-methoxy-N'-methylamide 

Downstream Products

• 1262483-19-1 C₂₇H₃₈N₂O₅ 
• 1262483-71-5 C₄₃H₅₆N₂O₅Si 

Relevant articles and documents

Peptidotriazolamers Inhibit Aβ(1–42) Oligomerization and Cross a Blood-Brain-Barrier Model

In peptidotriazolamers every second peptide bond is replaced by a 1H-1,2,3-triazole. Such foldamers are expected to bridge the gap in molecular weight between small-molecule drugs and protein-based drugs. Amyloid β (Aβ) aggregates play an important role in Alzheimer's disease. We studied the impact of amide bond replacements by 1,4-disubstituted 1H-1,2,3-triazoles on the inhibitory activity of the aggregation “hot spots” K16LVFF20 and G39VVIA42 in Aβ(1–42). We found that peptidotriazolamers act as modulators of the Aβ(1–42) oligomerization. Some peptidotriazolamers are able to interfere with the formation of toxic early Aβ oligomers, depending on the position of the triazoles, which is also supported by computational studies. Preliminary in vitro results demonstrate that a highly active peptidotriazolamer is also able to cross the blood-brain-barrier.

Enzymatic Macrocyclization of 1,2,3-Triazole Peptide Mimetics

The macrocyclization of linear peptides is very often accompanied by significant improvements in their stability and biological activity. Many strategies are available for their chemical macrocyclization, however, enzyme-mediated methods remain of great interest in terms of synthetic utility. To date, known macrocyclization enzymes have been shown to be active on both peptide and protein substrates. Here we show that the macrocyclization enzyme of the cyanobactin family, PatGmac, is capable of macrocyclizing substrates with one, two, or three 1,4-substituted 1,2,3-triazole moieties. The introduction of non-peptidic scaffolds into macrocycles is highly desirable in tuning the activity and physical properties of peptidic macrocycles. We have isolated and fully characterized nine non-natural triazole-containing cyclic peptides, a further ten molecules are also synthesized. PatGmac has now been shown to be an effective and versatile tool for the ring closure by peptide bond formation.

1,2,3-Triazole Stabilized Neurotensin-Based Radiopeptidomimetics for Improved Tumor Targeting

Neurotensin (NT) is a regulatory peptide with nanomolar affinity toward NT receptors, which are overexpressed by different clinically relevant tumors. Its binding sequence, NT(8-13), represents a promising vector for the development of peptidic radiotracers for tumor imaging and therapy. The main drawback of the peptide is its short biological half-life due to rapid proteolysis in vivo. Herein, we present an innovative strategy for the stabilization of peptides using nonhydrolizable 1,4-disubstituted, 1,2,3-triazoles as amide bond surrogates. A triazole scan?of the peptide sequence yielded novel NT(8-13) analogues with enhanced stability, retained receptor affinity, and improved tumor targeting properties in vivo. The synthesis of libraries of triazole-based peptidomimetics was achieved efficiently on solid support by a combination of Fmoc-peptide chemistry, diazo transfer reactions, and the Cu(I)-catalyzed alkyne azide cycloaddition (CuAAC) employing methods that are fully compatible with standard solid phase peptide synthesis (SPPS) chemistry. Thus, the amide-to-triazole substitution strategy may represent a general methodology for the metabolic stabilization of biologically active peptides.

Braces for the peptide backbone: Insights into structure-activity relationships of protease inhibitor mimics with locked amide conformations

Flower power: Potent protease inhibitors containing triazolyl mimics of cis and trans backbone amides were engineered based on the structure of the sunflower trypsin inhibitor 1. The biologically relevant cis-Pro motif was successfully replaced with a non

Dipeptide Mimics, Libraries Combining Two Dipeptide Mimics with a Third Group, and Methods for Production Thereof

Monovalent compounds having moieties comprising at least one amino acid side chain are bound to a core molecule, which also comprises a nucleophilic moiety bound to said core molecule. Monovalent compounds also comprise a macrocyclic ring, a nucleophilic

Universal peptidomimetics

This paper concerns peptidomimetic scaffolds that can present side chains in conformations resembling those of amino acids in secondary structures without incurring excessive entropic or enthalpic penalties. Compounds of this type are referred to here as minimalist mimics. The core hypothesis of this paper is that small sets of such scaffolds can be designed to analogue local pairs of amino acids (including noncontiguous ones) in any secondary structure; i.e., they are universal peptidomimetics. To illustrate this concept, we designed a set of four peptidomimetic scaffolds. Libraries based on them were made bearing side chains corresponding to many of the protein-derived amino acids. Modeling experiments were performed to give an indication of kinetic and thermodynamic accessibilities of conformations that can mimic secondary structures. Together, peptidomimetics based on these four scaffolds can adopt conformations that resemble almost any combination of local amino acid side chains in any secondary structure. Universal peptidomimetics of this kind are likely to be most useful in the design of libraries for high-throughput screening against diverse targets. Consequently, data arising from submission of these molecules to the NIH Molecular Libraries Small Molecule Repository (MLSMR) are outlined.

Histone deacetylase inhibitors: Synthesis of cyclic tetrapeptides and their triazole analogs

Synthesis of nine macrocyclic peptide HDAC inhibitors and three triazole derivatives is described. HDAC inhibitory activity of these compounds against HeLa cell lysate is evaluated. The biological data demonstrate that incorporation of a triazole unit improves the HDAC inhibitory activity.

A new stereoselective synthesis of chiral γ-functionalized (E)-allylic amines

Chiral t-Boc protected propargylic amines have been obtained starting from aminoaldehydes derived from natural aminoacids. Stannylcupration of these substrates affords an easy regio- and stereocontrolled route to the corresponding γ-stannylated (E)-allylamines which are useful intermediates for the synthesis of the corresponding γ-functionalized allylic systems.