73397-26-9

Basic information

• Product Name: BOC-(2R,3R)-3-AMINO-2-HYDROXY-5-METHYLHEXANOIC ACID
• Synonyms: N-BOC-(2R,3R)-2-HYDROXY-3-AMINO-5-METHYLHEXANOIC ACID;(2R,3R)-3-BOC-AMINO-2-HYDROXY-5-METHYLHEXANOIC ACID;BOC-(2R,3R)-3-AMINO-2-HYDROXY-5-METHYLHEXANOIC ACID;BOC-(2R,3R)-AHMH-OH;(2R,3R)-3-((tert-butoxycarbonyl)aMino)-2-hydroxy-5-Methylhexanoic acid
• CAS NO: 73397-26-9
• Molecular Formula: C₁₂H₂₃NO₅
• Molecular Weight: 261.31
• Mol File: 73397-26-9.mol
• Article Data: 2

Chemical Properties

• Appearance: /
• CAS DataBase Reference: BOC-(2R,3R)-3-AMINO-2-HYDROXY-5-METHYLHEXANOIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: BOC-(2R,3R)-3-AMINO-2-HYDROXY-5-METHYLHEXANOIC ACID(73397-26-9)
• EPA Substance Registry System: BOC-(2R,3R)-3-AMINO-2-HYDROXY-5-METHYLHEXANOIC ACID(73397-26-9)

Safety Data

• HazardClass: IRRITANT
• Hazardous Substances Data: 73397-26-9(Hazardous Substances Data)

Usage

General Description

BOC-(2R,3R)-3-amino-2-hydroxy-5-methylhexanoic acid is a chemical compound that belongs to the class of amino acids. It is a derivative of the amino acid leucine, which plays a crucial role in protein synthesis and muscle growth. BOC-(2R,3R)-3-amino-2-hydroxy-5-methylhexanoic acid is commonly used in peptide synthesis as a protecting group for the amino acid, allowing for selective manipulation of specific functional groups in the peptide chain. Its structure contains an amino group, a hydroxy group, and a methyl group, making it useful for the creation of diverse peptide sequences. Additionally, this compound provides increased stability to peptides during synthesis and purification processes. Overall, BOC-(2R,3R)-3-amino-2-hydroxy-5-methylhexanoic acid is essential in the production of peptides and plays a critical role in chemical and biochemical research.

Upstream product

• 1070-19-5 N-(tert-butyloxycarbonyl) azide 
• 62023-30-7 DL-threo-3-amino-2-hydroxy-5-methylhexanoic acid 
• 62023-30-7 (2RS,3R)-3-Amino-2-hydroxy-5-methylhexanoic Acid 
• 73397-30-5 (2R,3R)-3-<<(tert-Butyloxy)carbonyl>amino>-2-hydroxy-5-methylhexanoic Acid Methyl Ester 
• 70853-26-8 (R)-4-methyl-1-oxopentane-2-benzylcarbamate 
• 63219-62-5 [(S)-1-((S)-Cyano-hydroxy-methyl)-3-methyl-butyl]-carbamic acid benzyl ester 
• 73397-25-8 (2RS,3R)-3-<<(tert-Butyloxy)carbonyl>amino>-2-hydroxy-5-methylhexanoic Acid 
• 73397-22-5 Cbz-D-Leu-OMe 
• 875322-16-0 C₁₂H₂₃NO₂ 

Downstream Products

• 73397-34-9 (2S,3R)-<3-<<(tert-Butyloxy)carbonyl>amino>-2-hydroxy-5-methylhexanoyl>-L-valyl-L-valyl-aspartic Acid Dibenzyl Ester 
• 73465-22-2 (2R,3R)-<3-<<(tert-Butyloxy)carbonyl>amino>-2-hydroxy-5-methylhexanoyl>-L-valyl-L-valyl-aspartic Acid Dibenzyl Ester 
• 318464-20-9 (2R,3S)-3-amino-2-hydroxy-5-methylhexanoic acid 
• 73397-20-3 (2S,3S)-3-Amino-2-hydroxy-5-methylhexanoic Acid 
• 73397-27-0 (2S,3S)-3-[(tert-butoxycarbonyl)amino]-2-hydroxy-5-methylhexanoic acid 
• 73397-25-8 (2S,3R)-3-<<(tert-Butyloxy)carbonyl>amino>-2-hydroxy-5-methylhexanoic Acid 
• 73465-23-3 (2R,3R)-(3-Amino-2-hydroxy-5-methylhexanoyl)-L-valyl-L-valyl-L-aspartic Acid 
• 67655-94-1 amastatin 

Relevant articles and documents

Synthesis of new (-)-bestatin-based inhibitor libraries reveals a novel binding mode in the S1 pocket of the essential malaria M1 metalloaminopeptidase

The malarial PfA-M1 metallo-aminopeptidase is considered a putative drug target. The natural product dipeptide mimetic, bestatin, is a potent inhibitor of PfA-M1. Herein we present a new, efficient, and high-yielding protocol for the synthesis of bestatin derivatives from natural and unnatural N-Boc-d-amino acids. A diverse library of bestatin derivatives was synthesized with variants at the side chain of either the α-hydroxyβ-amino acid (P1) or the adjacent naturalα-amino acid (P1′). Surprisingly, we found that extended aromatic side chains at the P1 position resulted in potent inhibition against PfA-M1. To understand these data, we determined the X-ray cocrystal structures of PfA-M1 with two derivatives having either a Tyr(OMe) 15 or Tyr(OBzl) 16 at the P1 position and observed substantial inhibitor-induced rearrangement of the primary loop within the PfA-M1 pocket that interacts with the P1 side chain. Our data provide important insights for the rational design of more potent and selective inhibitors of this enzyme that may eventually lead to new therapies for malaria.