70853-19-9

Usage

InChI:InChI=1/C28H36N2O7/c1-19(2)24(30-27(34)37-28(3,4)5)25(32)29-22(26(33)36-18-21-14-10-7-11-15-21)16-23(31)35-17-20-12-8-6-9-13-20/h6-15,19,22,24H,16-18H2,1-5H3,(H,29,32)(H,30,34)

Upstream product

• 13734-41-3 t-Boc-L-valine 
• 2886-33-1 dibenzyl L-aspartate toluene-4-sulphonate 
• 2791-79-9 dibenzyl L-aspartate 

Downstream Products

• 70853-22-4 <(tert-Butyloxy)carbonyl>-L-valyl-L-valyl-L-aspartic Acid Dibenzyl Ester 
• 70853-20-2 Val-Asp(OBzl)-OBzl 
• 73465-23-3 (2R,3R)-(3-Amino-2-hydroxy-5-methylhexanoyl)-L-valyl-L-valyl-L-aspartic Acid 
• 67655-94-1 amastatin 
• 70853-23-5 Val-Val-Asp(OBzl)-OBzl 
• 69400-55-1 <(2R,3S)-3-Amino-2-hydroxy-5-methylhexanoyl>-L-Val-L-Val-L-Asp 
• 69400-55-1 <(2S,3S)-3-Amino-2-hydroxy-5-methylhexanoyl>-L-Val-L-Val-L-Asp 
• 70853-21-3 L-valyl-L-aspartic acid dibenzyl ester TFA salt 

Relevant academic research and scientific papers

N-linked peptidoresorc[4]arene-based receptors as noncompetitive inhibitors for α-chymotrypsin

This paper deals with the design, synthesis, and evaluation of a new series of receptors for protein surface recognition. The design of these agents is based around the attachment of four constrained dipeptide chains onto a central resorc[4]arene scaffold. By varying the sequence, nature, and stereochemistry of the chains we prepared anionically functionalized N-linked peptidoresorc[4] arenes 12, 13, and 17 by Pd/C-catalyzed hydrogenation of the corresponding benzyl esters 10, 11, and 16. From this family of receptors we have identified noncompetitive inhibitors of α-chymotrypsin (ChT), which function by binding to the surface of the enzyme in the neighborhood of the active site cleft (Ki values ranging from 12.4 ± 5.1 μM for free carboxylic acid (+)-12b to 0.76 ± 0.14 μM for benzyl ester (-)-16a). For anionically functionalized receptors 12, 13, and 17 the ChT inhibition is based essentially on electrostatic interaction, and the bound enzyme can be released from the resorcarene surface by increasing the ionic strength, with its activity almost completely restored. For receptors with terminal benzyl ester groups (10 and 16) a hydrophobic network can be suggested.

Synthesis of (2S,3R)-3-Amino-2-hydroxy-5-methylhexanoic Acid Derivatives. Application to the Synthesis of Amastatin, an Inhibitor of Aminopeptidases

Methods are reported for the synthesis of optically pure derivatives of (2S,3R)-3-amino-2-hydroxy-5-methylhexanoic acid. -D-leucine methyl ester was reduced in 95percent yield with diisobutylaluminum hydride to the aldehyde which was converted via the cyanohydrin to (2RS,3R)-3-amino-2-hydroxy-5-methylhexanoic acid (AHMHA).The mixture of diastereomers was converted to the corresponding Boc-AHMHA methyl ester derivatives and separated by chromatography over silica gel.The optical purity of the diastereomers at C-3 was established by converting each to diastereomeric Boc-AHMHA-Leu-OMe and separating these dipeptides by chromatography.Pure (2S,3R)-Boc-AHMHA was coupled with valyl-valyl-aspartic acid dibenzyl ester by using dicyclohexylcarbodiimide/ 1-hydroxybenzotriazole in 63percent yield.The Boc group was removed by using trifluoroacetid acid, and the benzyl groups were removed by hydrogenolysis.The product, (2S,3R)-AHMHA-L-Val-L-Val-L-Asp, amastatin, was found to be identical with the natural product.