66039-56-3

Basic information

• Product Name: N(4)-acetylspermidine
• Synonyms: N(4)-acetylspermidine
• CAS NO: 66039-56-3
• Molecular Formula: C9H21N3O
• Molecular Weight: 187.28254
• Mol File: 66039-56-3.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 333°Cat760mmHg
• Flash Point: 155.2°C
• Appearance: /
• Density: 0.991g/cm³
• Vapor Pressure: 0.00014mmHg at 25°C
• Refractive Index: 1.489
• CAS DataBase Reference: N(4)-acetylspermidine(CAS DataBase Reference)
• NIST Chemistry Reference: N(4)-acetylspermidine(66039-56-3)
• EPA Substance Registry System: N(4)-acetylspermidine(66039-56-3)

Safety Data

• Hazardous Substances Data: 66039-56-3(Hazardous Substances Data)

Usage

InChI:InChI=1/C9H21N3O/c1-9(13)12(8-4-6-11)7-3-2-5-10/h2-8,10-11H2,1H3

Upstream product

• 126993-27-9 N-acetyl-N'-(t-butoxycarbonyl)-N'-[3-(t-butoxycarbonylamino)propyl]-1,4-butanediamine 
• 89965-56-0 <3-<<4-(carboxyamino)butyl>amino>propyl>carbamic acid, dibenzyl ester 
• 126993-26-8 Acetyl-(4-{acetyl-[3-(acetyl-tert-butoxycarbonyl-amino)-propyl]-amino}-butyl)-carbamic acid tert-butyl ester 
• 62371-83-9 N,N',N''-Triacetylspermidin 
• 124-20-9 N-(3-aminopropyl)-1,4-diaminobutane 
• 123348-77-6 {4-[Acetyl-(3-benzyloxycarbonylamino-propyl)-amino]-butyl}-carbamic acid benzyl ester 

Relevant articles and documents

Exploiting protein fluctuations at the active-site Gorge of human cholinesterases: Further optimization of the design strategy to develop extremely potent inhibitors

Protein conformational fluctuations are critical for biological functions, although the relationship between protein motion and function has yet to be fully explored. By a thorough bioinformatics analysis of cholinesterases (ChEs), we identified specific hot spots, responsible for protein fluctuations and functions, and those active-site residues that play a role in modulating the cooperative network among the key substructures. This drew the optimization of our design strategy to discover potent and reversible inhibitors of human acetylcholinesterase and butyrylcholinesterase (hAChE and hBuChE) that selectively interact with specific protein substructures. Accordingly, two tricyclic moieties differently spaced by functionalized linkers were investigated as molecular yardsticks to probe the finest interactions with specific hot spots in the hChE gorge. A number of SAR trends were identified, and the multisite inhibitors 3a and 3d were found to be the most potent inhibitors of hBuChE and hAChE known to date.

CONVENIENT ROUTES TO ALKYL-SUBSTITUTED POLYAMINES

Alkyl-substituted polyamines, valuable for biological studies, can be prepared from N-phenylmethoxycarbonyl-1,4-diaminobutane (1b) and N-phenylmethoxycarbonyl-4-azidobutanamine (4a) by utilising the following reactions: (i) reduction of the phenylmethoxycarbonyl group to methyl by borane and (ii) combination of the Staudinger and aza-Wittig reactions .