10030-31-6

Basic information

• Product Name: AC-PHE-PHE-OH
• Synonyms: ACETYL-L-DIPHENYLALANINE;AC-PHE-PHE-OH;N-ACETYL-L-PHE-PHE;N-(N-acetyl-3-phenyl-L-alanyl)-3-phenyl-L-alanine;Ac-L-Phe-L-Phe-OH;N-(N-Acetyl-L-phenylalanyl)-L-phenylalanine;N-Acetyl-L-Phe-L-Phe-OH;Einecs 233-078-1
• CAS NO: 10030-31-6
• Molecular Formula: C₂₀H₂₂N₂O₄
• Molecular Weight: 354.4
• EINECS: 233-078-1
• Mol File: 10030-31-6.mol

Chemical Properties

• Melting Point: 264-265 °C (decomp)
• Boiling Point: 692.3°Cat760mmHg
• Flash Point: 372.5°C
• Appearance: /
• Density: 1.225g/cm³
• Vapor Pressure: 4.02E-20mmHg at 25°C
• Refractive Index: 1.584
• Storage Temp.: -15°C
• PKA: 3.51±0.10(Predicted)
• CAS DataBase Reference: AC-PHE-PHE-OH(CAS DataBase Reference)
• NIST Chemistry Reference: AC-PHE-PHE-OH(10030-31-6)
• EPA Substance Registry System: AC-PHE-PHE-OH(10030-31-6)

Safety Data

• Hazardous Substances Data: 10030-31-6(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Research:
AC-PHE-PHE-OH is used as a reference standard in the development and testing of drugs and pharmaceuticals. Its role in understanding peptide bonding and protein structure aids in the design and optimization of therapeutic agents.
Used in Biochemistry and Molecular Biology Research:
In the field of biochemistry and molecular biology, AC-PHE-PHE-OH is employed as a research tool to study the physical and chemical properties of peptides. This knowledge is crucial for advancing our understanding of the mechanisms underlying various biological processes and diseases.
Used in Peptide Synthesis:
AC-PHE-PHE-OH serves as a reference standard in peptide synthesis, ensuring the accuracy and consistency of synthesized peptides. This is vital for the development of new therapeutic peptides and the study of their biological activities.
Used in Protein Structure Analysis:
AC-PHE-PHE-OH is utilized in the analysis of protein structure, providing insights into the folding, stability, and function of proteins. This information is essential for the development of drugs targeting specific protein structures and for understanding the molecular basis of various diseases.

InChI:InChI=1/C20H22N2O4/c1-14(23)21-17(12-15-8-4-2-5-9-15)19(24)22-18(20(25)26)13-16-10-6-3-7-11-16/h2-11,17-18H,12-13H2,1H3,(H,21,23)(H,22,24)(H,25,26)/t17-,18-/m0/s1

Upstream product

• 42291-22-5 N-acetyl dehydrophenylalanyl-(S)-phenylalanine 
• 78087-68-0 N-(α-acetylamino-cinnamoyl)-L-phenylalanine 
• 63-91-2 L-phenylalanine 
• 78087-67-9 Ac-ΔPhe-(R)-Phe-OH 
• 35661-40-6 N-Fmoc L-Phe 
• 108-24-7 acetic anhydride 
• 55604-95-0 N-acetyl-L-phenylalanine N-hydroxysuccinimide ester 
• 128992-42-7 N-Acetylphenylalanylphenylalanine tert-butyl ester 
• 15100-75-1 L-phenylalanine tert-butyl ester hydrochloride 
• 2577-40-4 Phe-Phe 
• 507-09-5 tiolacetic acid 
• 18934-57-1 N-acetyl-L-phenylalaninehydrazide 
• 2361-96-8 ethyl N-acetyl-(L)-phenylalaninate 
• 2018-61-3 (S)-2-acetylamino-3-phenylpropanoic acid 

Downstream Products

• 2562-48-3 N-acetyl-L-phenylalanyl-L-phenylalanine methylester 
• 1422538-40-6 C₄₆H₅₇N₇O₇ 

Relevant articles and documents

Facile synthesis of a peptidic Au(i)-metalloamphiphile and its self-assembly into luminescent micelles in water

We report a short synthetic route for the preparation of a peptidic Au(i)-metalloamphiphile which, in buffered environments of physiological ionic strength, self-assembles into luminescent micellar nanostructures of 14 nm in diameter. This journal is

A catalytic one-step synthesis of peptide thioacids: the synthesis of leuprorelin via iterative peptide-fragment coupling reactions

A catalytic one-step synthesis of peptide thioacids was developed. The oxygen-sulfur atom exchange reaction converted the carboxy group at the C-terminus of the peptides into a thiocarboxy group with suppressed epimerization. This method was successfully applied to the synthesis of the peptide drug leuprorelin via an iterative fragment-coupling protocol.

Evaporation-Induced Self-Assembly of Small Peptide-Conjugated Silica Nanoparticles

Self-assembly processes guide disordered molecules or particles into long-range organized structures due to specific supramolecular interactions among the building entities. Herein, we report a unique evaporation-induced self-assembly (EISA) strategy for four different silica nanoparticle systems obtained through peptide functionalization of the particle surface. First, covalent peptide-silica coupling was investigated in detail, starting with the grafting of a single amino acid (L-serine) and expanded to specific small peptides (up to four amino acids) and transferred to different particle types (MCM-48-type MSNs, solid nanoparticles, and newly developed virus-like nanoparticles). These materials were investigated regarding their ability to undergo EISA, which was shown to be independent of particle type and amount of peptide anchored to their surface. This EISA-based approach provides new possibilities for the design of future advanced drug delivery systems, engineered hierarchical sorbents, and nanocatalyst assemblies.

Electrostatic interaction and induced fitting of the rhodium(I) complex coordinated by diphosphine ligand having an amino group in the diastereoselective hydrogenation of dehydrodipeptides

Rhodium(I)-[2-[2-(dimethylamino)ethyl]-1,3-propanediyl]bis(diphenylphosphine) (DPP-AE) catalyst achieved an effective 1,4-asymmetric induction and afforded high diastereoselectivity (max. 96% d.e.) in the hydrogenation of dehydrodipeptides in protic solve

Tuning the mechanistic pathways of peptide self-assembly by aromatic interactions

Herein, we have unravelled the key influence of aromatic interactions on the mechanistic pathways of peptide self-assembly by introducing suitable chromophores (pyrenevs.naphthalene). Although both self-assembled peptides are indistinguishable in their mo

A traceless approach to amide and peptide construction from thioacids and dithiocarbamate-terminal amines

A novel and traceless strategy has been devised that allows a coupling of thioacids and dithiocarbamate-terminal amines. This strategy had been assumed to be dependent on the attachment of a functional equivalent of a cysteine side chain in earlier native chemical ligation approaches. This approach enables the traceless removal of CS2 to directly generate the desired amide bond and is compatible with a range of unprotected side chains of amino acid. The ability to produce amide or peptides by a traceless removal of the auxiliary is a significant virtue of the method. Meanwhile, the application of this new peptide-bond-forming reaction to the synthesis of novel endomorphin (EM) derivatives with various binding potencies was realized.

Phenylalanine racemization: A side reaction of dipeptide formation

It was shown that acetylated dipeptides, Ac-D-Phe-D-Phe-OH, Ac-L-Phe-L-Phe-OH, Ac-D-Phe-L-Phe-OH, and Ac-L-Phe-D-Phe-OH, are formed during D-phenylalanine racemization. The overall content of these dipeptides in the reaction mixture ranged from 40 to 60% depending on the reaction conditions. We concluded that, like α-aminoisobutyric acid, phenylalanine is prone to polymerization under racemization conditions.

Efficient 1,4-Asymetric Induction Utilizing Electrostatic Interaction between Ligand and Substrate in the Asymmetric Hydrogenation of Didehydrodipeptides

Electrostatic interaction between the amino group of the achiral 3-dimethylaminopropylidenebismethylenebis(diphenylphosphine) (1) and the carboxy group of the substrate enable an effective 1,4-asymmetric induction in the RhI-catalysed hydrogenation of didehydrodipeptides, to give (S,S)-or (R,R)-products selectively.The selectivity reached up to 94percent diastereoisomeric excess with acetyl didehydrodipeptides and 92percent with benzyloxycarbonyl substrates.

ASYMMETRIC HYDROGENATION WITH RHODIUM(I)-CHIRAL DIPHOSPHINITES. THE EFFECT OF THE DIMETHYLAMINO GROUP OF THE LIGAND ON THE ASYMMETRIC INDUCTION.

New chiral diphosphinites were prepared starting from ( plus )-diethyl tartrate. The asymmetric hydrogenation of dehydroamino acids, itaconic acid and dehydrodipeptides was studied using Rh(I)-diphosphinite catalysts. In the hydrogenation of dehydroamino acid derivatives, an introduction of omega -(dimethylamino)alkyl group in the ligands did not raise the optical yield. By the use of Rh(I)-diphosphinite having 3-(dimethylamino)propyl group the inversion of the preferred product was observed. 19 refs.