3235-46-9

Basic information

• Product Name: NSC20667
• Synonyms: NSC20667;4-amino-4-methylpentanoic acid(SALTDATA: HCl);4-amino-4-methyl-valeric acid;4-Amino-4-methylpentanoic acid hydrochloride
• CAS NO: 3235-46-9
• Molecular Formula: C₆H₁₃NO₂
• Molecular Weight: 131.17292
• Mol File: 3235-46-9.mol
• Article Data: 4

Chemical Properties

• Boiling Point: 241.4°Cat760mmHg
• Flash Point: 99.8°C
• Appearance: /
• Density: 1.041g/cm³
• Vapor Pressure: 0.012mmHg at 25°C
• Refractive Index: 1.466
• Storage Temp.: 2-8°C
• CAS DataBase Reference: NSC20667(CAS DataBase Reference)
• NIST Chemistry Reference: NSC20667(3235-46-9)
• EPA Substance Registry System: NSC20667(3235-46-9)

Safety Data

• HazardClass: IRRITANT
• Hazardous Substances Data: 3235-46-9(Hazardous Substances Data)

Usage

General Description

NSC20667 is a chemical compound that has been studied for its potential anti-cancer properties. It has been found to inhibit the proliferation of cancer cells and induce cell death in various cancer types, including breast, prostate, and leukemia. Research has also suggested that NSC20667 may have anti-inflammatory and neuroprotective effects, making it a potential candidate for the development of new treatments for cancer and other diseases. Further studies are needed to fully understand its mechanisms of action and potential therapeutic benefits.

InChI:InChI=1/C6H13NO2/c1-6(2,7)4-3-5(8)9/h3-4,7H2,1-2H3,(H,8,9)

Upstream product

• 5165-28-6 5,5-dimethyl-2-pyrrolidone 
• 16507-02-1 methyl 4-methyl-4-nitropentanoate 
• 5762-41-4 Benzyl-γ-nitro-γ-methylvalerat 

Relevant articles and documents

Effect of Differential Geminal Substitution of γAmino Acid Residues at the (i + 2) Position of αγTurn Segments on the Conformation of Template β-Hairpin Peptides

The effect of insertion of three geminally dimethyl substituted γamino acid residues [γ2,2 (4-amino-2,2-dimethylbutanoic acid), γ3,3 (4-amino-3,3-dimethylbutanoic acid), and γ4,4 (4-amino-4,4-dimethylbutanoic acid)] at the (i + 2) position of a two-residue αγC12 turn segment in a model octapeptide sequence Leu-Phe-Val-Aib-Xxx-Leu-Phe-Val (where Xxx = γamino acid residues) has been investigated in this study. Solution conformational studies (NMR, CD, and IR) and ab initio calculations indicated that γ3,3 and γ4,4 residues were well accommodated in the β-hairpin nucleating αγC12 turns, which gave rise to well-registered hairpins, in contrast to γ2,2, which was unable to form a tight C12 β-hairpin nucleating turn and promote a well-registered β-hairpin. Geminal disubstitution at the Cα carbon in γ2,2 led to unfavorable steric contacts, disabling its accommodation in the αγC12 hairpin nucleating turn unlike the γ3,3 and γ4,4 residues. Geminal substitutions at different carbons along the backbone constrained backbone torsion angles for the three γamino acid residues differently, generating diverse conformational preferences in them. Folded hairpins were energetically more stable (～8 to 9 kcal/mol) than the unfolded peptides. Conformational preference of the peptides was independent of the N-terminal protecting group. Such fundamental understanding will instrumentalize the future directed design of foldamers.

Straightforward synthesis of indolizidine alkaloid 167B

The synthetic access to indolizidines, substituted in C-5 position, was reported with good diastereoselectivity. The strategy developed was based on a key step of Michael addition associated with a Clauson-Kaas condensation.