180462-81-1

Basic information

• Product Name: Hydrazinecarboxylic acid, 2-(3-methylbutyl)-, 1,1-dimethylethyl ester (9CI)
• Synonyms: Hydrazinecarboxylic acid, 2-(3-methylbutyl)-, 1,1-dimethylethyl ester (9CI)
• CAS NO: 180462-81-1
• Molecular Formula: C₁₀H₂₂N₂O₂
• Molecular Weight: 202.29388
• Product Categories: N-BOC
• Mol File: 180462-81-1.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• CAS DataBase Reference: Hydrazinecarboxylic acid, 2-(3-methylbutyl)-, 1,1-dimethylethyl ester (9CI)(CAS DataBase Reference)
• NIST Chemistry Reference: Hydrazinecarboxylic acid, 2-(3-methylbutyl)-, 1,1-dimethylethyl ester (9CI)(180462-81-1)
• EPA Substance Registry System: Hydrazinecarboxylic acid, 2-(3-methylbutyl)-, 1,1-dimethylethyl ester (9CI)(180462-81-1)

Safety Data

• Hazardous Substances Data: 180462-81-1(Hazardous Substances Data)

Upstream product

• 590-86-3 isovaleraldehyde 
• 57699-53-3 N^α-isobutyl-N^β-Boc-hydrazine 
• 870-46-2 t-butoxycarbonylhydrazine 
• 180462-76-4 N'-(3-methylbutylidene)hydrazinecarboxylic acid tert-butyl ester 

Downstream Products

• 497155-20-1 [N'-tert-butoxycarbonyl-N-(3-methyl-butyl)-hydrazino]-phenyl-acetic acid 
• 180462-84-4 N'-((2S,3S)-3-tert-Butoxycarbonylamino-2-hydroxy-4-phenyl-butyl)-N'-(3-methyl-butyl)-hydrazinecarboxylic acid tert-butyl ester 

Relevant articles and documents

Falcipain inhibitors: Optimization studies of the 2-pyrimidinecarbonitrile lead series

Falcipain-2 and falcipain-3 are papain-family cysteine proteases of the malaria parasite Plasmodium falciparum that are responsible for host hemoglobin hydrolysis to provide amino acids for parasite protein synthesis. Different heteroarylnitrile derivatives were studied as potential falcipain inhibitors and therefore potential antiparasitic lead compounds, with the 5-substituted-2- cyanopyrimidine chemical class emerging as the most potent and promising lead series. Through a sequential lead optimization process considering the different positions present in the initial scaffold, nanomolar and subnanomolar inhibitors at falcipains 2 and 3 were identified, with activity against cultured parasites in the micromolar range. Introduction of protonable amines within lead molecules led to marked improvements of up to 1000 times in activity against cultured parasites without noteworthy alterations in other SAR tendencies. Optimized compounds presented enzymatic activities in the picomolar to low nanomolar range and antiparasitic activities in the low nanomolar range.

Aza-peptide analogs as potent human immunodeficiency virus type-1 protease inhibitors with oral bioavailability

A series of aza-peptide analogs with a (hydroxyethyl)hydrazine isostere has been synthesized as HIV-1 protease inhibitors using a simple synthetic scheme. Structure-activity studies based on the X-ray of a previously described inhibitor-enzyme complex led to potent inhibitors with antiviral activity in the low-nanomolar range. The S-configuration of the transition- state hydroxyl group was preferred in this series. Small modifications of the P2P3 and P2'P3' substituents had little effect on enzyme inhibition but greatly influenced the pharmacokinetic profile. As a result of these studies, the symmetrically acylated compound 8a and its close analog 24a bearing a methyl carbamate in P3 and an ethyl carbamate in P3' position were identified as potent inhibitors with plasma concentrations exceeding antiviral ED50 values 150-fold following oral application in mice.