135673-97-1

Basic information

• Product Name: FMOC-CHA-OH
• Synonyms: FMOC-3-CYCLOHEXYL-L-ALANINE;FMOC-BETA-CYCLOHEXYL-ALANINE;FMOC-BETA-CYCLOHEXYL-ALA-OH;FMOC-BETA-CYCLOHEXYL-L-ALANINE;FMOC-CHA-OH;FMOC-L-3-CYCLOHEXYLALANINE;FMOC-L-CYCLOHEXYLALANINE;FMOC-L-CHA-OH
• CAS NO: 135673-97-1
• Molecular Formula: C₂₄H₂₇NO₄
• Molecular Weight: 393.48
• Product Categories: Amino Acids;Peptide;Unusual Amino Acids - Ala
• Mol File: 135673-97-1.mol

Chemical Properties

• Melting Point: 125-130°C
• Boiling Point: 517.93°C (rough estimate)
• Flash Point: 323 °C
• Appearance: /Solid
• Density: 1.1836 (rough estimate)
• Refractive Index: 1.6000 (estimate)
• Storage Temp.: 2-8°C
• Solubility: soluble in Dimethylformamide
• PKA: 3.91±0.10(Predicted)
• BRN: 7052264
• CAS DataBase Reference: FMOC-CHA-OH(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-CHA-OH(135673-97-1)
• EPA Substance Registry System: FMOC-CHA-OH(135673-97-1)

Safety Data

• Statements: 36/37/38
• Safety Statements: 22-24/25-35-44-28-7-4
• WGK Germany: 3
• F: 10
• HazardClass: IRRITANT
• Hazardous Substances Data: 135673-97-1(Hazardous Substances Data)

Usage

Chemical Properties

White powder

Uses

Fmoc-Cha-OH,

Upstream product

• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 4441-50-3 L-2-cyclohexylalanine 
• 27527-05-5 L-cyclohexylalanine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 

Downstream Products

• 148982-99-4 ((S)-1-tert-Butylcarbamoyl-2-cyclohexyl-ethyl)-carbamic acid 9H-fluoren-9-ylmethyl ester 

Relevant articles and documents

Fungal Dioxygenase AsqJ Is Promiscuous and Bimodal: Substrate-Directed Formation of Quinolones versus Quinazolinones

Previous studies showed that the FeII/α-ketoglutarate dependent dioxygenase AsqJ induces a skeletal rearrangement in viridicatin biosynthesis in Aspergillus nidulans, generating a quinolone scaffold from benzo[1,4]diazepine-2,5-dione substrates. We report that AsqJ catalyzes an additional, entirely different reaction, simply by a change in substituent in the benzodiazepinedione substrate. This new mechanism is established by substrate screening, application of functional probes, and computational analysis. AsqJ excises H2CO from the heterocyclic ring structure of suitable benzo[1,4]diazepine-2,5-dione substrates to generate quinazolinones. This novel AsqJ catalysis pathway is governed by a single substituent within the complex substrate. This unique substrate-directed reactivity of AsqJ enables the targeted biocatalytic generation of either quinolones or quinazolinones, two alkaloid frameworks of exceptional biomedical relevance.

Single Amino-Acid Based Self-Assembled Biomaterials with Potent Antimicrobial Activity

The design and development of soft biomaterials based on amino acid and short-peptide have gained much attention due to their potent biomedical applications. A slight alteration in the side-chain of single amino acid in a peptide or protein sequence has a huge impact on the structure and function. Phenylalanine is one of the most studied amino acids, which contains an aromatic phenyl group connected through a flexible ?CH2? unit. In this work, we have examined whether flexibility and aromatic functionality of phenylalanine (Phe) are important in gel formation of model gelator Fmoc-Phe-OH or not. To examine this hypothesis, we synthesized Fmoc-derivatives of three analogues unnatural amino acids including cyclohexylalanine, phenylglycine, and homophenylalanine; which are slightly varied from Phe. Interestingly, all these three new analogues formed hydrogels in phosphate buffer at pH 7.0 having different gelation efficacy and kinetics. This study suggests that the presence of aromatic side-chain and flexibility are not mandatory for the gelation of this model gelator. Newly synthesized unnatural amino acid derivatives have also exhibited promising antimicrobial activity towards gram-positive bacteria by inhibiting cellular oxygen consumption. We further determined the biocompatibility of these amino acid derivatives by using a hemolysis assay on human blood cells. Overall studies described the development of single amino acid-based new injectable biomaterials with improved antimicrobial activity by the slight alteration in the side-chain of amino acid.

Method for identifying an enzyme to design anti-cancer compounds

The present invention relates to a method for identification of enzymes that are preferentially expressed in certain tumor tissue as compared with rapidly growing normal cells or tissue, use of said enzymes for the compound design to generate an active anti-cancer substance selectively in tumor tissue, compounds designed based on said enzymes, their pharmaceutically acceptable salts as well as pharmaceutical composition thereof.

Site-specific incorporation of non-natural residues into peptides: Effect of residue structure on suppression and translation efficiencies

A systematic survey of the structural requirements for biosynthetic incorporation of non-natural residues into a polypeptide is presented. Relative translation efficiencies for a series of 12 semi-synthetic acylated suppressor tRNAs ranged from 0 to 91% depending on the structure of the residue incorporated.