118429-74-6

Basic information

• Product Name: H-Asp(OBzl)-Asp(OBzl)-OBzl
• Synonyms: H-Asp(OBzl)-Asp(OBzl)-OBzl
• CAS NO: 118429-74-6
• Molecular Weight: 518.566
• Mol File: 118429-74-6.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: H-Asp(OBzl)-Asp(OBzl)-OBzl(CAS DataBase Reference)
• NIST Chemistry Reference: H-Asp(OBzl)-Asp(OBzl)-OBzl(118429-74-6)
• EPA Substance Registry System: H-Asp(OBzl)-Asp(OBzl)-OBzl(118429-74-6)

Safety Data

• Hazardous Substances Data: 118429-74-6(Hazardous Substances Data)

Upstream product

• 58471-53-7 (S)-2-((S)-2-Amino-3-carboxy-propionylamino)-succinic acid 
• 100-51-6 benzyl alcohol 
• 13798-75-9 N^α-t-butoxycarbonylaspartic acid α-N-hydroxysuccinimide ester β-benzyl ester 
• 2886-33-1 dibenzyl L-aspartate toluene-4-sulphonate 
• 7536-58-5 BOC-L-aspartic acid 4-benzyl ester 

Downstream Products

• 107208-63-9 L-Asp-L-Asp-L-Asp-OH 
• 104870-33-9 Ac-Asp(OBzl)-Asp(OBzl)-OBzl 

Relevant articles and documents

Carbonic anhydrase activators: Human isozyme II is strongly activated by oligopeptides incorporating the carboxyterminal sequence of the bicarbonate anion exchanger AE1

Di-/tri- and especially tetrapeptides incorporating the sequence DADD present in the carboxyterminal region of the bicarbonate/chloride anion exchanger AE1 strongly activate human carbonic anhydrase (CA) isozyme II, whereas they act as more inefficient ac

Synthesis of acyclic and dehydroaspartic acid analogues of Ac-Asp-Glu-OH and their inhibition of rat brain N-acetylated α-linked acidic dipeptidase (NAALA dipeptidase)

The following structural and conformationally constrained analogues of Ac-Asp-Glu-OH (1) were synthesized: Ac-Glu-Glu-OH (2), Ac-D-Asp-Glu-OH (3), Ac-Glu-Asp-OH (4), Ac-Asp-Asp-OH (5), Ac-Asp-3-aminohexanedioic acid (6), Ac-3-amino-3-(carboxymethyl)propanoyl-Glu-OH (7), N-succinyl-Glu-OH (8), N-maleyl-Glu-OH (9), N-fumaryl-Glu-OH (10), and Ac-Δ(z)Asp-Glu-OH (11). These analogues were evaluated for their ability to inhibit the hydrolysis of Ac-Asp-[3,4-3H]-Glu-OH by N-acetylated α-linked acidic dipeptidase (NAALA dipeptidase) in order to gain some insight into the structural requirements for the inhibition of this enzyme. Analogues 4-6 and 9 were very weak inhibitors of NAALA dipeptidase (K(i) > 40 μM), while 2, 3, and 7 with K(i) values ranging from 3.2-8.5 μM showed intermediate inhibitory activity. The most active inhibitors of NAALA dipeptidase were compounds 8, 10, and 11 with K(i) values of 0.9, 0.4, and 1.4 μM, respectively. These results suggest that the relative spacing between the side chain carboxyl and the α-carboxyl group of the C-terminal residue may be important for binding to the active site of the enzyme. They also indicate that the χ1 torsional angle for the aspartyl residue is in the vicinity of 0°.