116662-96-5

Basic information

• Product Name: tert-butyl (R)-1-formyl-3-methylbutylcarbamate
• Synonyms: tert-butyl (R)-1-formyl-3-methylbutylcarbamate
• CAS NO: 116662-96-5
• Molecular Formula: C₁₁H₂₁NO₃
• Molecular Weight: 215.28934
• Mol File: 116662-96-5.mol
• Article Data: 14

Chemical Properties

• Appearance: /
• CAS DataBase Reference: tert-butyl (R)-1-formyl-3-methylbutylcarbamate(CAS DataBase Reference)
• NIST Chemistry Reference: tert-butyl (R)-1-formyl-3-methylbutylcarbamate(116662-96-5)
• EPA Substance Registry System: tert-butyl (R)-1-formyl-3-methylbutylcarbamate(116662-96-5)

Safety Data

• Hazardous Substances Data: 116662-96-5(Hazardous Substances Data)

Upstream product

• 129603-01-6 (R)-N^α-(tert-butoxycarbonyl)-N-methoxy-N-methylleucinamide 
• 106930-51-2 tert-butyl [(2R)-1-hydroxy-4-methylpentan-2-yl]carbamate 
• 133467-01-3 methyl (2R)-2-(tert-butoxycarbonylamino)-4-methylpentanoate 
• 87694-50-6 N-(tert-butoxycarbonyl)-L-leucine-N'-methoxy-N'-methylamide 
• 16937-99-8 N-Boc-D-Leu 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 200937-21-9 (R)-Boc-leucine hydrate 

Downstream Products

• 129603-19-6 (S)-2-methyl-4-aminononane hydrochloride 
• 1356606-82-0 (R)-3-(((9H-fluoren-9-yl)methoxy)carbonylamino)-2-hydroxy-5-methylhexanoic acid 
• 1426828-69-4 (3S,4R)-allyl 4-[(S)-2-(tert-butoxycarbonylamino)-3-(tritylthio)propanamido]-3-(tert-butyldimethylsiloxy)-6-methylheptanoate 
• 1426828-65-0 (3S,4R)-allyl 4-[(S)-2-amino-3-(tritylthio)propanamido]-3-(tert-butyldimethylsiloxy)-6-methylheptanoate 

Relevant articles and documents

Antibiotic N′,N″-dibenzyleremomycin with a reduced 1,2-peptide bond

Eremomycin derivatives with benzylated amino groups of both residues of eremosamine and with (R) or (S)-2-amino-4-methylpentyl substituted for N-methyl-D-Leu, the first amino acid residue of its heptapeptide, were synthesized in order to study the role of

Binding cooperativity between a ligand carbonyl group and a hydrophobic side chain can be enhanced by additional H-bonds in a distance dependent manner: A case study with thrombin inhibitors

One of the underappreciated non-covalent binding factors, which can significantly affect ligand-protein binding affinity, is the cooperativity between ligand functional groups. Using four different series of thrombin inhibitors, we reveal a strong positiv

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.