138754-84-4

Basic information

• Product Name: Carbamic acid, (1-formyl-2-methylpropyl)-, phenylmethyl ester, (R)-
• CAS NO: 138754-84-4
• Molecular Formula: C13H17NO3
• Molecular Weight: 235.283
• Mol File: 138754-84-4.mol
• Article Data: 42

Chemical Properties

• CAS DataBase Reference: Carbamic acid, (1-formyl-2-methylpropyl)-, phenylmethyl ester, (R)-(CAS DataBase Reference)
• NIST Chemistry Reference: Carbamic acid, (1-formyl-2-methylpropyl)-, phenylmethyl ester, (R)-(138754-84-4)
• EPA Substance Registry System: Carbamic acid, (1-formyl-2-methylpropyl)-, phenylmethyl ester, (R)-(138754-84-4)

Safety Data

• Hazardous Substances Data: 138754-84-4(Hazardous Substances Data)

Upstream product

• 178614-85-2 (S)-3-benzyloxycarbonyl-4-isopropyl-2,5-oxazolidinedione 
• 24210-19-3 methyl (2S)-3-methyl-[(benzyloxy)carbonylamino]butanoate 
• 95500-74-6 N-Benzyloxycarbonyl-L-valinal diethylacetal 
• 6192-52-5 p-toluenesulfonic acid monohydrate 
• 67436-18-4 N-benzyloxycarbonyl-S-valine methyl ester 
• 13139-17-8 N-(Benzyloxycarbonyloxy)succinimide 
• 260978-43-6 benzyl (1R)-1-(hydroxymethyl)-2-methylpropylcarbamate 
• 4467-55-4 N-Z-D-valine N-hydroxysuccinimide ester 
• 41445-88-9 (2-methylpropoxy)carbonyl N-[(benzyloxy)carbonyl]-D-valinate 
• 154674-66-5 (2S,5R,3E)-2-(Benzyloxymethoxy)-6-methyl-5-(benzyloxycarbonylamino)hept-3-ene 
• 2026-48-4 (S)-valinol 
• 501-53-1 benzyl chloroformate 
• 72-18-4 L-valine 
• 17498-50-9 L-valine hydrochloride 

Downstream Products

• 143914-86-7 (E)-(S)-4-Benzyloxycarbonylamino-2,5-dimethyl-hex-2-enoic acid ethyl ester 
• 796039-35-5 (4S)-4-benzyloxycarbonylamino-5-methylhex-2-enoic acid methyl ester 
• 848983-56-2 (E)-(S)-4-Benzyloxycarbonylamino-5-methyl-hex-2-enoic acid ethyl ester 
• 111854-83-2 ((Z)-(S)-4-Hydroxy-1-isopropyl-but-2-enyl)-carbamic acid benzyl ester 
• 1009587-34-1 (1R,3S,1'S)-1-[1'-[(N-benzyloxycarbonyl)amino]-2'-methyl-propyl]-1,2,3,4-tetrahydro-β-carboline-3-carboxylic acid methyl ester 
• 1009587-58-9 (1S,3S,1'R)-1-[1'-[(N-benzyloxycarbonyl)amino]-2'-methyl-propyl]-1,2,3,4-tetrahydro-β-carboline-3-carboxylic acid methyl ester 
• 1449512-59-7 (S)-(N-hydroxy-3-oxobutanoylaminomethyl-2-methylpropyl)carbamic acid benzyl ester 
• 1449512-57-5 (S)-2-benzyloxycarbonylamino-3-methylbutanaldoxime 

Relevant articles and documents

Discovery of (Dihydro)pyrazine N-Oxides via Genome Mining in Pseudomonas

Overexpression of the Pseudomonas virulence factor (pvf) biosynthetic operon led to the identification of a family of pyrazine N-oxides (PNOs), including a novel dihydropyrazine N,N′-dioxide (dPNO) metabolite. The nonribosomal peptide synthetase responsib

Synthetic method of key intermediate Tuv of natural anti-cancer drug Tubulysins

The invention belongs to the technical field of chemical synthesis, and particularly relates to a synthesis method of a key intermediate Tuv of a natural anti-cancer drug Tubulysins. With L-valinol (1) which is cheap and easy to obtain as a raw material,

Discovery of Peptidomimetic Antibody-Drug Conjugate Linkers with Enhanced Protease Specificity

Antibody-drug conjugates (ADCs) have become an important therapeutic modality for oncology, with three approved by the FDA and over 60 others in clinical trials. Despite the progress, improvements in ADC therapeutic index are desired. Peptide-based ADC linkers that are cleaved by lysosomal proteases have shown sufficient stability in serum and effective payload-release in targeted cells. If the linker can be preferentially hydrolyzed by tumor-specific proteases, safety margin may improve. However, the use of peptide-based linkers limits our ability to modulate protease specificity. Here we report the structure-guided discovery of novel, nonpeptidic ADC linkers. We show that a cyclobutane-1,1-dicarboxamide-containing linker is hydrolyzed predominantly by cathepsin B while the valine-citrulline dipeptide linker is not. ADCs bearing the nonpeptidic linker are as efficacious and stable in vivo as those with the dipeptide linker. Our results strongly support the application of the peptidomimetic linker and present new opportunities for improving the selectivity of ADCs.