87512-31-0

Basic information

• Product Name: FMOC-ALA-ALA-OH
• Synonyms: Fmoc-L-Ala-L-Ala-OH;(S)-2-((S)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)propanamido)propanoic acid;Fmoc-Ala-Ala-OH99%;FMOC-ALA-ALA-OH;FMOC-L-ALANYL-L-ALANINE;FMoc-AA-OH;N-[(9H-Fluoren-9-ylmethoxy)carbonyl]-L-alanyl-L-alanine;FMoc-Ala-Ala
• CAS NO: 87512-31-0
• Molecular Formula: C₂₁H₂₂N₂O₅
• Molecular Weight: 382.41
• Mol File: 87512-31-0.mol
• Article Data: 13

Chemical Properties

• Melting Point: 175-179℃ (ethyl acetate hexane )
• Boiling Point: 674.2±45.0 °C(Predicted)
• Appearance: /
• Density: 1.280±0.06 g/cm3(Predicted)
• Storage Temp.: -15°C
• PKA: 3.49±0.10(Predicted)
• CAS DataBase Reference: FMOC-ALA-ALA-OH(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-ALA-ALA-OH(87512-31-0)
• EPA Substance Registry System: FMOC-ALA-ALA-OH(87512-31-0)

Safety Data

• Hazardous Substances Data: 87512-31-0(Hazardous Substances Data)

Usage

General Description

FMOC-ALA-ALA-OH is a chemical compound used as a building block in the synthesis of peptides. It consists of three amino acids, specifically alanine, arranged in a chain and protected by a fluorenylmethyloxycarbonyl (FMOC) group. The FMOC group serves to protect the amino acids during peptide synthesis and can be easily removed in the final step. FMOC-ALA-ALA-OH is commonly used in solid-phase peptide synthesis as a precursor to create longer, more complex peptides with specific amino acid sequences. FMOC-ALA-ALA-OH is widely used in the research and development of pharmaceuticals and biochemistry due to its versatile applications in peptide chemistry.

Upstream product

• 56-41-7 L-alanin 
• 86060-86-8 (9H-fluoren-9-yl-methoxy)carbonyl-L-alanine pentafluorophenyl ester 
• 35661-39-3 N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 
• 93709-88-7 Nα-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanyl-L-alanine methyl ester 
• 73724-40-0 (S)-2,5-dioxopyrrolidin-1-yl 2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)propanoate 
• 1948-31-8 di-L-alanine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 161009-04-7 N-α-(9-fluorenylmethoxycarbonyl)-di-L-alanine tert-butyl ester 

Downstream Products

• 697805-40-6 C₅₁H₅₈FN₇O₁₀ 
• 1438853-39-4 N^α-Fmoc-Ala-Ala-Asn(N-trityl)-PABC-PNP 

Relevant articles and documents

Alaninyl variants of the marine natural product halocyamine A and their antibacterial properties

In an effort to explore the antibacterial potential of the marine natural product halocyamine A, a series of analogues including desbromo and alanine-substituted variants were synthesised and evaluated for biological activity against a panel of Gram-positive and –negative bacteria. The analogues were synthesised by a combination of solid-phase peptide synthesis and ruthenium complex/ytterbium triflate catalysed hydroamidation chemistry. Single alanine substitutions ([Ala1]-halocyamine A and [Ala2]-halocyamine A) gave only modest increases in activity towards Gram-positive bacteria, while di-alaninyl variants exhibited more potent activity with MIC values of 12.5–50 μM towards the Gram-positive bacteria Staphylococcus aureus and Enterococcus faecalis. A lipophilic trityl-protected intermediate of [Ala2]-halocyamine was the most active against the Gram-negative bacterium Escherichia coli.

ANTI-EGFR ANTIBODY DRUG CONJUGATES

The invention relates to anti-Epidermal Growth Factor Receptor (EGFR) antibody drug conjugates (ADCs) which inhibit Bcl-xL, including compositions and methods of using said ADCs.

Localized Supramolecular Peptide Self-Assembly Directed by Enzyme-Induced Proton Gradients

Electrodes are ideal substrates for surface localized self-assembly processes. Spatiotemporal control over such processes is generally directed through the release of ions generated by redox reactions occurring specifically at the electrode. The so-used gradients of ions proved their effectiveness over the last decade but are in essence limited to material-based electrodes, considerably reducing the scope of applications. Herein is described a strategy to enzymatically generate proton gradients from non-conductive surfaces. In the presence of oxygen, immobilization of glucose oxidase (GOx) on a multilayer film provides a flow of protons through enzymatic oxidation of glucose by GOx. The confined acidic environment located at the solid–liquid interface allows the self-assembly of Fmoc-AA-OH (Fmoc=fluorenylmethyloxycarbonyl and A=alanine) dipeptides into β-sheet nanofibers exclusively from and near the surface. In the absence of oxygen, a multilayer nanoreactor containing GOx and horseradish peroxidase (HRP) similarly induces Fmoc-AA-OH self-assembly.