35661-38-2

Basic information

• Product Name: FMOC-DL-ALA-OH
• Synonyms: FMOC-DL-ALA-OH;Alanine,N-[(9H-fluoren-9-ylmethoxy)carbonyl]-;Fmoc-DL-Ala;(9H-Fluoren-9-yl)MethOxy]Carbonyl DL-Ala-OH
• CAS NO: 35661-38-2
• Molecular Formula: C₁₈H₁₇NO₄
• Molecular Weight: 311.335
• Mol File: 35661-38-2.mol
• Article Data: 12

Chemical Properties

• Boiling Point: 544.1±33.0 °C(Predicted)
• Appearance: /
• Density: 1.282±0.06 g/cm3(Predicted)
• Storage Temp.: 2-8°C
• PKA: 3.91±0.10(Predicted)
• CAS DataBase Reference: FMOC-DL-ALA-OH(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-DL-ALA-OH(35661-38-2)
• EPA Substance Registry System: FMOC-DL-ALA-OH(35661-38-2)

Safety Data

• Hazardous Substances Data: 35661-38-2(Hazardous Substances Data)

Usage

General Description

FMOC-DL-ALA-OH is a compound consisting of FMOC (9-fluorenylmethoxycarbonyl), DL-ALA (DL-alanine), and OH (hydroxyl) groups. FMOC is a protective group commonly used in peptide synthesis to protect the amine group of amino acids. DL-ALA is a racemic mixture of the amino acid alanine, which is a proteinogenic amino acid with diverse biological functions. The OH group indicates that the compound has a hydroxyl functional group, which can contribute to its solubility and reactivity. FMOC-DL-ALA-OH is often used as a building block in peptide chemistry and pharmaceutical research for the synthesis of peptide-based drugs and materials.

Upstream product

• 71953-00-9 2-(9H-Fluoren-9-ylmethoxycarbonylamino)-propionic acid tert-butyl ester 
• 338-69-2 D-Alanine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 35661-38-2 Fmoc-alanine 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 1227363-07-6 (LGACAGL)2 
• 1227363-09-8 (AACAA)2 
• 302-72-7 rac-Ala-OH 
• 909114-66-5 9-fluorenylmethyl 4,6-dimethoxy-1,3,5-triazinyl carbonate 

Downstream Products

• 183444-88-4 D-(N-9-fluorenylmethoxycarbonylalanyl)-L-phenylalanine tert-butyl ester 
• 215872-24-5 (R)-2-{(S)-2-[(S)-2-Acetylamino-3-(4-benzyloxy-phenyl)-propionylamino]-3-methyl-butyrylamino}-propionic acid 
• 136391-83-8 Ac-6Bpa-Thr-Pro-D-Ala-Val-Phe-NH₂ 
• 136391-82-7 Ac-6Bpa-Thr-Pro-D-Ala-Val-6Bpa-NH₂ 
• 1104388-40-0 C₅₇H₈₇N₃O₇ 
• 1104388-26-2 C₅₄H₈₂N₂O₆ 
• 1272660-84-0 (2R,1'R)-2-benzyl-1-benzyloxycarbonyl-2-[(1'-carbamoyl)ethyl]carbamoylazetidine 
• 1272660-83-9 (2S,1'R)-2-benzyl-1-benzyloxycarbonyl-2-[(1'-carbamoyl)ethyl]carbamoylazetidine 
• 201864-71-3 (R)-3-((fluorenylmethoxycarbonyl)amino)butyric acid 
• 174756-44-6 FCE 28073 

Relevant articles and documents

COMPOUND FOR PREPARATION OF ANTIBODY-PAYLOAD CONJUGATE AND USE THEREOF

The present application relates to a novel linker for use in bioconjugation, comprising two or more electrophilic carbon atoms of a carbonyl group, and a click chemistry functional group and, more specifically, to a linker through which a compound, a peptide, and/or a protein can be directly and/or indirectly linked by a substitution reaction to a desired target molecule, that is, a target molecule.

Novel chiral stationary phases based on 3,5-dimethyl phenylcarbamoylated β-cyclodextrin combining cinchona alkaloid moiety

Novel chiral selectors based on 3,5-dimethyl phenylcarbamoylated β-cyclodextrin connecting quinine (QN) or quinidine (QD) moiety were synthesized and immobilized on silica gel. Their chromatographic performances were investigated by comparing to the 3,5-dimethyl phenylcarbamoylated β-cyclodextrin (β-CD) chiral stationary phase (CSP) and 9-O-(tert-butylcarbamoyl)-QN-based CSP (QN-AX). Fmoc-protected amino acids, chiral drug cloprostenol (which has been successfully employed in veterinary medicine), and neutral chiral analytes were evaluated on CSPs, and the results showed that the novel CSPs characterized as both enantioseparation capabilities of CD-based CSP and QN/QD-based CSPs have broader application range than β-CD-based CSP or QN/QD-based CSPs. It was found that QN/QD moieties play a dominant role in the overall enantioseparation process of Fmoc-amino acids accompanied by the synergistic effect of β-CD moiety, which lead to the different enantioseparation of β-CD-QN-based CSP and β-CD-QD-based CSP. Furthermore, new CSPs retain extraordinary enantioseparation of cyclodextrin-based CSP for some neutral analytes on normal phase and even exhibit better enantioseparation than the corresponding β-CD-based CSP for certain samples.

Structure-guided engineering of: Meso -diaminopimelate dehydrogenase for enantioselective reductive amination of sterically bulky 2-keto acids

meso-Diaminopimelate dehydrogenase (DAPDH) and mutant enzymes are an excellent choice of biocatalysts for the conversion of 2-keto acids to the corresponding d-amino acids. However, their application in the enantioselective reductive amination of bulky 2-keto acids, such as phenylglyoxylic acid, 2-oxo-4-phenylbutyric acid, and indole-3-pyruvic acid, is still challenging. In this study, the structure-guided site-saturation mutagenesis of a Symbiobacterium thermophilum DAPDH (StDAPDH) gave rise to a double-site mutant W121L/H227I, which showed dramatically improved enzyme activities towards various 2-keto acids including these sterically bulky substrates. Several d-amino acids were prepared in optically pure form. The molecular docking of substrates into the active sites of wild-type and mutant W121L/H227I enzymes revealed that the substrate binding cavity of the mutant enzyme was reshaped to accommodate these bulky substrates, thus leading to higher enzyme activity. These results lay a foundation for further shaping the substrate binding pocket and manipulating the interactions between the substrate and binding sites to access highly active d-amino acid dehydrogenases for the preparation of synthetically challenging d-amino acids.