21708-31-6

Basic information

• Product Name: 9-(3-aminopropyl)-9H-purin-6-amine
• Synonyms: 9-(3-Aminopropyl)-9H-purin-6-amine; 9H-purine-9-propanamine, 6-amino-
• CAS NO: 21708-31-6
• Molecular Formula: C₈H₁₂N₆
• Molecular Weight: 192.2211
• Mol File: 21708-31-6.mol
• Article Data: 6

Chemical Properties

• Boiling Point: 444°C at 760 mmHg
• Flash Point: 222.3°C
• Density: 1.56g/cm³
• Vapor Pressure: 4.42E-08mmHg at 25°C
• Refractive Index: 1.774
• CAS DataBase Reference: 9-(3-aminopropyl)-9H-purin-6-amine(CAS DataBase Reference)
• NIST Chemistry Reference: 9-(3-aminopropyl)-9H-purin-6-amine(21708-31-6)
• EPA Substance Registry System: 9-(3-aminopropyl)-9H-purin-6-amine(21708-31-6)

Safety Data

• Hazardous Substances Data: 21708-31-6(Hazardous Substances Data)

Upstream product

• 83948-53-2 3-bromopropylamine tert-butylcarbamate 
• 73-24-5 7H-purin-6-ylamine 
• 19255-49-3 9-(3-chloropropyl)-9H-purin-6-amine 
• 66224-66-6 adenine 
• 675608-70-5 9-(3-azidopropyl)adenine 

Downstream Products

• 79953-24-5 6-chloro-2-methoxy-9-<(3-(aden-9-yl)propyl)amino>acridine 
• 675608-87-4 9-(2-{bis[(diphenylphosphanoyl)methyl]amino}propyl)adenine 
• 1241981-19-0 3-(benzyloxycarbonyl-L-leucylamino)-N-(3-(6-amino-9H-purin-9-yl)propyl)-2-oxophenylbutanamide 
• 1241981-18-9 3-(benzyloxycarbonyl-L-leucylamino)-N-(3-(6-amino-9H-purin-9-yl)propyl)-2-oxopentanamide 
• 1052678-02-0 3-(benzyloxycarbonyl-L-leucylamino)-N-(3-(6-amino-9H-purin-9-yl)propyl)-2-oxo-pentanamide 
• 675608-86-3 9-(3-(bis[(diphenylphosphanoyl)methyl]amino)propyl)adenine 
• 120075-69-6 [3-(6-Amino-purin-9-yl)-propyl]-(5-benzyloxy-6-methoxy-quinazolin-4-yl)-amine 

Relevant articles and documents

Shear Stress-Responsive Polymersome Nanoreactors Inspired by the Marine Bioluminescence of Dinoflagellates

Some marine plankton called dinoflagellates emit light in response to the movement of surrounding water, resulting in a phenomenon called milky seas or sea sparkle. The underlying concept, a shear-stress induced permeabilisation of biocatalytic reaction compartments, is transferred to polymer-based nanoreactors. Amphiphilic block copolymers that carry nucleobases in their hydrophobic block are self-assembled into polymersomes. The membrane of the vesicles can be transiently switched between an impermeable and a semipermeable state by shear forces occurring in flow or during turbulent mixing of polymersome dispersions. Nucleobase pairs in the hydrophobic leaflet separate when mechanical force is applied, exposing their hydrogen bonding motifs and therefore making the membrane less hydrophobic and more permeable for water soluble compounds. This polarity switch is used to release payload of the polymersomes on demand, and to activate biocatalytic reactions in the interior of the polymersomes.

FORCE-RESPONSIVE POLYMERSOMES AND NANOREACTORS; PROCESSES UTILIZING THE SAME

The mechanically induced melting properties of DNA were employed to achieve force labile membranes is described. Nucleobase pairs were used as mechanophores. Adenine and thymine functionalized complementary amphiphilic block copolymers were self-assembled

Cocrystal structures of primed side-extending α-ketoamide inhibitors reveal novel calpain-inhibitor aromatic interactions

Calpains are intracellular cysteine proteases that catalyze the cleavage of target proteins in response to Ca2+ signaling. When Ca2+ homeostasis is disrupted, calpain overactivation causes unregulated proteolysis, which can contribute to diseases such as postischemic injury and cataract formation. Potent calpain inhibitors exist, but of these many cross-react with other cysteine proteases and will need modification to specifically target calpain. Here, we present crystal structures of rat calpain 1 protease core (μI-II) bound to two α-ketoamide-based calpain inhibitors containing adenyl and piperazyl primed-side extensions. An unexpected aromatic-stacking interaction is observed between the primed-side adenine moiety and the Trp298 side chain. This interaction increased the potency of the inhibitor toward μI-II and heterodimeric m-calpain. Moreover, stacking orients the adenine such that it can be used as a scaffold for designing novel primed-side address regions, which could be incorporated into future inhibitors to enhance their calpain specificity.