17136-28-6

Basic information

• Product Name: H-BETA-ALA-PHE-OH
• Synonyms: H-BETA-ALA-PHE-OH;BETA-ALA-PHE;B-ALA-PHE;beta-alanyl-phenylalanine;H-b-Ala-Phe-OH
• CAS NO: 17136-28-6
• Molecular Formula: C₁₂H₁₆N₂O₃
• Molecular Weight: 236.27
• Product Categories: Dipeptides;Dipeptides and Tripeptides;Peptides
• Mol File: 17136-28-6.mol

Chemical Properties

• Melting Point: 253-255 °C (decomp)
• Boiling Point: 506.8°Cat760mmHg
• Flash Point: 260.3°C
• Appearance: /
• Density: 1.224g/cm³
• Vapor Pressure: 4.31E-11mmHg at 25°C
• Refractive Index: 1.567
• Storage Temp.: −20°C
• PKA: 3.45±0.10(Predicted)
• CAS DataBase Reference: H-BETA-ALA-PHE-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-BETA-ALA-PHE-OH(17136-28-6)
• EPA Substance Registry System: H-BETA-ALA-PHE-OH(17136-28-6)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 17136-28-6(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
H-BETA-ALA-PHE-OH is used as a potential therapeutic agent for modulating biological processes and interacting with specific cellular receptors, which may lead to the development of new drugs and therapies for various medical conditions.
Used in Biochemical Research:
H-BETA-ALA-PHE-OH is used as a research tool for studying protein structure and function, aiding in the understanding of the molecular mechanisms underlying various biological processes.
Used in Synthesis of Bioactive Compounds:
H-BETA-ALA-PHE-OH is utilized in the synthesis of other bioactive compounds, potentially leading to the discovery of new pharmaceutical agents with diverse applications in medicine.

InChI:InChI=1/C12H16N2O3/c13-7-6-11(15)14-10(12(16)17)8-9-4-2-1-3-5-9/h1-5,10H,6-8,13H2,(H,14,15)(H,16,17)

Upstream product

• 63-91-2 L-phenylalanine 
• 672912-22-0 Boc-β-Ala-L-Phe-OMe 
• 936124-44-6 Boc-β-Ala-L-Phe-OH 

Downstream Products

• 612844-05-0 (S)-2-(3-azidopropanamido)-3-phenylpropanoic acid 

Relevant articles and documents

A new molecular scaffold for the formation of supramolecular peptide double helices: The crystallographic insight

A series of water-soluble synthetic dipeptides (1-3) with an N-terminally located β-alanine residue, β-alanyl-L-valine (1), β-alanyl-L- isoleucine (2), and β-alanyl-L-phenylalanine (3), form hydrogen-bonded supramolecular double helices with a pitch length of 1 nm, whereas the C-terminally positioned β-alanine containing dipeptide (4), L-phenylalanyl-β-alanine, does not form a supramolecular double helical structure. β-Ala-Xaa (Xaa = Val/lle/Phe) can be regarded as a new motif for the formation of supramolecular double helical structures in the solid state.

Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase: A strategy for the design of peptidase inhibitors

The cholecystokinin-8 (CCK-8)-inactivating peptidase is a serine peptidase which has been shown to be a membrane-bound isoform of tripeptidyl peptidase II (EC 3.4.14.10). It cleaves the neurotransmitter CCK-8 sulfate at the Met-Gly bond to give Asp-Tyr(SO3H)-Met-OH + Gly-Trp-Met-Asp-Phe-NH2. In seeking a reversible inhibitor of this peptidase, the enzymatic binding subsites were characterized using a fluorimetric assay based on the hydrolysis of the artificial substrate Ala-Ala-Phe-amidomethylcoumarin. A series of di- and tripeptides having various alkyl or aryl side chains was studied to determine the accessible volume for binding and to probe the potential for hydrophobic interactions. From this initial study the tripeptides Ile-Pro-Ile-OH (K(i) = 1 μM) and Ala-Pro-Ala-OH (K(i) = 3 μM) and dipeptide amide Val-Nvl-NHBu (K(i) = 3 μM) emerged as leads. Comparison of these structures led to the synthesis of Val-Pro-NHBu (K(i) = 0.57 μM) which served for later optimization in the design of butabindide, a potent reversible competitive and selective inhibitor of the CCK-8-inactivating peptidase. The strategy for this work is explicitly described since it illustrates a possible general approach for peptidase inhibitor design.