26488-24-4

Basic information

• Product Name: phenylalanyl-prolyl diketopiperazine
• Synonyms: phenylalanyl-prolyl diketopiperazine;Cyclo(D-Phe-L-Pro);(3R,8aS)-Hexahydro-3-(phenylmethyl)pyrrolo[1,2-a]pyrazine-1,4-dione;Pyrrolo[1,2-a]pyrazine-1,4-dione, hexahydro-3-(phenylmethyl)-, (3R,8aS)-
• CAS NO: 26488-24-4
• Molecular Formula: C₁₄H₁₆N₂O₂
• Molecular Weight: 244.29
• Mol File: 26488-24-4.mol
• Article Data: 30

Chemical Properties

• Melting Point: 153-157℃
• Boiling Point: 509.5°Cat760mmHg
• Flash Point: 262°C
• Appearance: /
• Density: 1.26g/cm³
• CAS DataBase Reference: phenylalanyl-prolyl diketopiperazine(CAS DataBase Reference)
• NIST Chemistry Reference: phenylalanyl-prolyl diketopiperazine(26488-24-4)
• EPA Substance Registry System: phenylalanyl-prolyl diketopiperazine(26488-24-4)

Safety Data

• Hazardous Substances Data: 26488-24-4(Hazardous Substances Data)

Usage

General Description

Phenylalanyl-prolyl diketopiperazine is a dipeptide molecule composed of the amino acids phenylalanine and proline. It is a cyclic compound formed by the condensation of these two amino acids and is often found in certain foods and beverages, such as beer and bread. This molecule has been studied for its potential health effects, including its role in the human gastrointestinal system and its possible anti-inflammatory properties. Additionally, phenylalanyl-prolyl diketopiperazine has been investigated for its potential use in drug delivery systems and as a marker for food quality and safety. Overall, this compound has sparked interest in the scientific community for its various biological activities and potential applications in food and pharmaceutical industries.

Upstream product

• 67-64-1 acetone 
• 69936-03-4 (1S)-methyl 2-[(S)-2-amino-3-phenylpropanoyl]cyclopentanecarboxylate 
• 15761-39-4 1-(tert-butoxycarbonyl)-L-proline 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 83825-04-1 L-phenylalanine-L-proline methyl ester 
• 100-39-0 benzyl bromide 
• 21685-51-8 D-phenylalanine methyl ester 
• 94779-08-5 Boc-Pro-D-Phe-OH 
• 63-91-2 L-phenylalanine 
• 1170674-20-0 (2S)-2-amino-3-[4-(prop-2-ynyloxy)phenyl]-propionic acid 
• 3978-80-1 Boc-Tyr-OH 
• 783333-86-8 (2S)-2-tert-butoxycarbonylamino-3-[4-(prop-2-ynyloxy)phenyl]-propionic acid propargyl ester 
• 113568-21-1 (BOC)2Phe-OH 
• 147-85-3 L-proline 

Downstream Products

• 78452-05-8 [(S)-1-((S)-3-Benzyl-1,4-dioxo-hexahydro-pyrrolo[1,2-a]pyrazine-2-carbonyl)-2-methyl-propyl]-carbamic acid tert-butyl ester 
• 78452-05-8 [(S)-1-((S)-3-Benzyl-1,4-dioxo-hexahydro-pyrrolo[1,2-a]pyrazine-2-carbonyl)-2-methyl-propyl]-carbamic acid tert-butyl ester 
• 81531-47-7 [(S)-2-((S)-3-Benzyl-1,4-dioxo-hexahydro-pyrrolo[1,2-a]pyrazin-2-yl)-1-benzyloxymethyl-2-oxo-ethyl]-carbamic acid tert-butyl ester 
• 3705-26-8 L-Phenylalanyl-D-prolin-lactam 
• 50868-53-6 N-(d-Lysergyl-L-valyl)-L-phenylalanyl-L-prolin-lactam 
• 78452-06-9 [(S)-1-((3S,8aS)-3-Benzyl-1,4-dioxo-hexahydro-pyrrolo[1,2-a]pyrazine-2-carbonyl)-2-methyl-propyl]-carbamic acid benzyl ester 
• 96625-34-2 N--Phe-Pro-Lactam 
• 50868-53-6 N-(d-Lysergyl-L-valyl)-L-phenylalanyl-L-prolin-lactam 
• 78452-05-8 [(S)-1-((3S,8aS)-3-Benzyl-1,4-dioxo-hexahydro-pyrrolo[1,2-a]pyrazine-2-carbonyl)-2-methyl-propyl]-carbamic acid tert-butyl ester 
• 81531-47-7 N--Phe-Pro-Lactam 
• 32021-26-4 3-benzylhexahydropyrrolo[1,2-a]pyrazin-1,4-dione 
• 128425-02-5 L-FDAA-L-Pro 
• 673-06-3 D-(R)-phenylalanine 
• 95713-61-4 L-FDAA-D-Phe 

Relevant articles and documents

Unambiguous stereochemical assignment of cyclo(Phe-pro), cyclo(leu-pro), and cyclo(val-pro) by electronic circular dichroic spectroscopy

2,5-diketopiperazines (DKPs) are cyclic dipeptides ubiquitously found in nature. In particular, cyclo(Phe-Pro), cyclo(Leu-Pro), and cyclo(Val-Pro) are frequently detected in many microbial cultures. Each of these DKPs has four possible stereoisomers due to the presence of two chirality centers. However, absolute configurations of natural DKPs are often ambiguous due to the lack of a simple, sensitive, and reproducible method for stereochemical assignment. This is an important problem because stereochemistry is a key determinant of biological activity. Here, we report a synthetic DKP library containing all stereoisomers of cyclo(Phe-Pro), cyclo(Leu-Pro), and cyclo(Val-Pro). The library was subjected to spectroscopic characterization using mass spectrometry, NMR, and electronic circular dichroism (ECD). It turned out that ECD can clearly differentiate DKP stereoisomers. Thus, our ECD dataset can serve as a reference for unambiguous stereochemical assignment of cyclo(Phe-Pro), cyclo(Leu-Pro), and cyclo(Val-Pro) samples from natural sources. The DKP library was also subjected to a biological screening using assays for E. coli growth and biofilm formation, which revealed distinct biological effects of cyclo(D-Phe-L-Pro).

Antidiabetic in vitro and in vivo evaluation of cyclodipeptides isolated from Pseudomonas fluorescens IB-MR-66e

Three cyclodipeptides [cyclo(l-Pro-l-Leu), 1; cyclo(l-Pro-l-Val), 2; and cyclo(l-Pro-l-Phe), 3] were isolated from Pseudomonas fluorescens IB-MR-66e. The structures were established by spectral means and corroborated by synthesis. The antidiabetic potential of compounds 1-3 was explored in vivo, in vitro and in silico. The three peptides showed important inhibitory activity against the α-glucosidase enzyme. Further analysis in vivo using a sucrose tolerance test corroborated that compounds 1 and 3 (1-30 mg kg-1) significantly reduced the postprandial state. Peptide 1 (1-30 mg kg-1) also reduced the postprandial peak after a glucose challenge and exhibited significant hypoglycemia during an insulin tolerance test; thus, its antidiabetic action involved also an improvement of insulin utilization not related to Akt phosphorylation nor to an increment in mitochondrial bioenergetics nor insulin secretion.

Reprogramming nonribosomal peptide synthetases for "clickable" amino acids

Nonribosomal peptide synthetases (NRPSs) are multifunctional enzymes that produce a wide array of bioactive peptides. Here we show that a single tryptophan-to-serine mutation in phenylalanine-specific NRPS adenylation domains enables the efficient activat