26060-97-9

Basic information

• Product Name: N-decanoylphenylalanine
• CAS NO: 26060-97-9
• Molecular Formula: C₁₉H₂₉NO₃
• Molecular Weight: 319.4385
• Mol File: 26060-97-9.mol

Chemical Properties

• Boiling Point: 519.4°C at 760 mmHg
• Flash Point: 267.9°C
• Density: 1.048g/cm³
• Vapor Pressure: 1.29E-11mmHg at 25°C
• Refractive Index: 1.515
• CAS DataBase Reference: N-decanoylphenylalanine(CAS DataBase Reference)
• NIST Chemistry Reference: N-decanoylphenylalanine(26060-97-9)
• EPA Substance Registry System: N-decanoylphenylalanine(26060-97-9)

Safety Data

• Hazardous Substances Data: 26060-97-9(Hazardous Substances Data)

Usage

Uses

Used in Biochemistry:
N-decanoylphenylalanine is used as a modified amino acid for research purposes in the field of biochemistry. Its unique structure allows for the investigation of its interactions with other molecules and its potential role in various biochemical processes.
Used in Pharmaceutical Industry:
N-decanoylphenylalanine is used as a potential therapeutic agent for the development of new drugs. Its structural modification may provide novel properties that could be beneficial in the treatment of certain diseases or conditions, making it a valuable compound for pharmaceutical research and development.

Upstream product

• 334-48-5 1-decanoic acid 
• 63-91-2 L-phenylalanine 
• 75536-39-9 L-N-decanoylphenylalanine p-nitrophenyl ester 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 2577-90-4 methyl (2S)-2-amino-3-phenylpropanoate 
• 112-13-0 n-decanoyl chloride 
• 75531-06-5 2-Decanoylamino-3-phenyl-propionic acid 4-nitro-phenyl ester 
• 75531-06-5 2-Decanoylamino-3-phenyl-propionic acid 4-nitro-phenyl ester 

Downstream Products

• 1569832-28-5 (S)-2-(decylamino)-3-phenylpropan-1-ol 

Relevant articles and documents

New antimicrobial self-assembling short lipopeptides

Lipopeptides are an exceptional example of amphiphilic molecules that self-assemble into functional structures with applications in the areas of nanotechnology, catalysis or medicinal chemistry. Herein, we report a library of 21 short lipopeptides, together with their supramolecular characterization and antimicrobial activity against both Gram-negative (E. coli) and Gram-positive (S. aureus) strains. This study shows that simple lipoamino acids self-assemble into micellar or vesicular structures, while incorporating dipeptides capable of stablishing hydrogen bonds results in the adoption of advanced fibrilar structures. The self-assembly effect has proven to be key to achieve antimicrobial activity.

Mechanoresponsive, proteolytically stable and biocompatible supergelators from ultra short enantiomeric peptides with sustained drug release propensity

Stimuli-responsive low molecular weight hydrogelators attract immense interest from diverse segments of biomedicine and biotechnology. Distinctly, herein we report newly synthesized enantiomeric ultrashort peptides of general formula Me-(CH2)8-CO-NH-CH(X)-COOH, where X = CH2Ph in hydrogelators I (l-Phe) and II (d-Phe) respectively, which display excellent self-assembling propensity in physiological buffer at room temperature. Interestingly these biomolecules were endowed with mechanoresponsiveness, injectability and high mechanical integrity as confirmed by rheological measurements. Importantly they revealed resistance towards proteolytic degradation. Indeed dose dependent cell viability studies using MTT assay in four different cell lines, namely PANC-1, S1, HCT-116 and MDAMB-231, further confirmed the biocompatibility of the hydrogelators in vitro. The structural aspect of β-sheets of the hydrogelators was concluded on the basis of temperature dependent NMR, IR, PXRD and computational studies. We developed a user friendly delivery system, hydrogel nanoparticles (HNPs), with our mechanoresponsive and biocompatible hydrogelators, as these particles exhibited promising influence due to their enhanced surface area. Also the HNPs revealed excellent drug release kinetics for the model drugs 5FU/doxorubicin under physiological conditions in a sustained manner depending on the physicochemical parameters of the drugs. Taking these results together we envision that our designed hydrogelators and the delivery vehicle generated therefrom might represent a promising tool for administration of significant drug concentrations at lesion sites for a prolonged period, thus providing a better strategy for quick pain relief, rapid recovery and reduced systemic side effects.

Antibacterial lipopeptides and methods for their preparation and use

Novel antibacterial lipopeptides, pharmaceutical compositions, and methods for their preparation and use are described.

Direct Hydroxylation of Benzene to Phenol by Cytochrome P450BM3 Triggered by Amino Acid Derivatives

The selective hydroxylation of benzene to phenol, without the formation of side products resulting from overoxidation, is catalyzed by cytochrome P450BM3 with the assistance of amino acid derivatives as decoy molecules. The catalytic turnover rate and the total turnover number reached 259 min?1 P450BM3?1 and 40 200 P450BM3?1 when N-heptyl-l-proline modified with l-phenylalanine (C7-l-Pro-l-Phe) was used as the decoy molecule. This work shows that amino acid derivatives with a totally different structure from fatty acids can be used as decoy molecules for aromatic hydroxylation by wild-type P450BM3. This method for non-native substrate hydroxylation by wild-type P450BM3 has the potential to expand the utility of P450BM3 for biotransformations.

Novel stereoselective incorporation and hydrolysis of long-chain amino-acid substrates by vesicular membrane systems which include tri- or tetra-peptide catalysts

In the vesicular membrane system comprising N,N-didodecyl-N,N-dimethylammonium bromide and tri- and or tetra-peptide catalysts (pH 7.68; ionic strength μ = 0.15; 298 K), Z-L-Leu-L-His-L-Leu (or Z-L-Leu-L-His-L-Leu-L-Leu), having a hydrophobic terminal L-l

Enantioselective Hydrolysis of N-Acyl Amino Acid Esters by Tripeptide-type L-Histidine Derivative in a Bilayer Vesicular System

Peculiar enantioselective hydrolysis of N-acyl amino acid esters was found in the bilayer vesicular systems containing the tripeptide-type histidine derivative, Z-L-Leu-L-His-L-Leu.The enantioselectivity for the hydrolysis of long chain N-acyl phenylalanine p-nitrophenyl ester, C16-Phe-PNP, appeared in the binding process and was governed by an entropy factor.

Enantioselective Catalysis of Deacylation of p-Nitrophenyl N-Acylphenylalanates by Mixed Micelles composed of Nα-Hexadecanoyl-L-histidine and a Cationic Surfactant

The deacylation of p-nitrophenyl N-acyl-L and -D-phenylalanates (acyl=acetyl, decanoyl, and hexadecanoyl) with the co-micellar system composed of Nα-hexadecanoyl-L-histidine and octadecyltrimethylammonium chloride was investigated for the 20-35

STEREOSELECTIVE DEACYLATION OF LONG-CHAIN p-NITROPHENYL N-ACYLPHENYLALANATES BY PALMITOYL-L-HISTIDINE IN A BILAYER SYSTEM

In the stereoselective deacylation of H-n-1 -CONHCH(CH2Ph)CO2-C6H4NO2-p (n=10 and 16), the bilayer catalytic systems of palmitoyl-L-histidine and double-chain surfactants (2N2Br; m=12 and 14) offered the relatively higher enantiomer rat