36238-67-2

Basic information

• Product Name: Cyclo[D-Leu-L-Pro-]
• Synonyms: (3R,8aS)-Octahydro-3-(2-methylpropyl)pyrrolo[1,2-a]pyrazine-1,4-dione;Cyclo[D-Leu-L-Pro-];(3R,8aS)-Hexahydro-3-(2-methylpropyl)pyrrolo[1,2-a]pyrazine-1,4-dione;Cyclo(L-prolyl-D-leucyl);Cyclo(S-Pro-R-Leu);Cyclo-L-prolyl-D-leucine;Hexahydro-3-(2-methylpropyl)-pyrrolo[1,2-a]pyrazine-1,4-dione
• CAS NO: 36238-67-2
• Molecular Formula: C₁₁H₁₈N₂O₂
• Molecular Weight: 210.27
• Mol File: 36238-67-2.mol
• Article Data: 6

Chemical Properties

• Melting Point: 154-157℃
• Appearance: /
• CAS DataBase Reference: Cyclo[D-Leu-L-Pro-](CAS DataBase Reference)
• NIST Chemistry Reference: Cyclo[D-Leu-L-Pro-](36238-67-2)
• EPA Substance Registry System: Cyclo[D-Leu-L-Pro-](36238-67-2)

Safety Data

• Hazardous Substances Data: 36238-67-2(Hazardous Substances Data)

Usage

Description

Cyclo[D-Leu-L-Pro-], also known as Cyclo(D-Leu-L-Pro), is a cyclic dipeptide composed of D-leucine and L-proline amino acids. It is derived from marine-derived bacteria and has a unique cyclic structure that contributes to its biological activity.

Uses

Used in Pharmaceutical Industry:
Cyclo[D-Leu-L-Pro-] is used as an inhibitory agent for secretory group IIa phospholipase A2. This enzyme plays a crucial role in inflammatory processes and is associated with various diseases, including rheumatoid arthritis and asthma. The inhibitory effect of Cyclo[D-Leu-L-Pro-] on this enzyme helps in reducing inflammation and managing the symptoms of these diseases.
Additionally, Cyclo[D-Leu-L-Pro-] may have potential applications in other industries, such as cosmetics or food and beverage, due to its antimicrobial properties. However, more research is needed to explore these applications fully.

Upstream product

• 75188-89-5 L-prolyl-L-leucylglycylglycine 
• 52899-07-7 L-prolyl-L-leucine 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 96163-72-3 ethyl proline hydrochloride 
• 116939-86-7 ((benzyloxy)carbonyl)-L-leucyl-L-proline 
• 1380332-79-5 cyclo(Z-L-Leu-D-Pro) 
• 1380332-87-5 Cbz-(L)-leucyl-(D)-prolyl benzotriazole 
• 1380332-71-7 Cbz-(L)-leucyl-(L)-prolyl benzotriazole 
• 2018-66-8 Z-Leu-OH 
• 2899-43-6 DL-leucine ethyl ester 

Downstream Products

• 1072102-31-8 (8aR)-3c-isobutyl-(8ar)-octahydro-pyrrolo[1,2-a]pyrazine 
• 61-90-5 L-leucine 
• 147-85-3 L-proline 

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).

AGRICULTURAL CHEMICAL CONTAINING 2,5-DIKETOPIPERAZINE DERIVATIVE AS ACTIVE INGREDIENT

Disclosed herein is an agricultural agent containing a 2,5-diketopiperazine derivative capable of controlling plant diseases and promoting plant growth or an agriculturally acceptable salt thereof as an active ingredient.

Model studies of competing hydrolysis and epimerization of some tetrapeptides of interest in amino acid racemization studies in geochronology

The processes of epimerization of individual peptide units in proteins and the concurrent cleavage of peptide bonds are modelled by heating some tetrapeptide and tetrapeptide derivatives to 148.5 deg C in pH 6.8 phosphate buffer.An excess of D-proline was observed during the heating of L-propyl-L-leucylglycylglycine.The D/L ratio of proline attains a maximum value of 2.1 after 90 minutes.The excess D-proline is attributed to the formation of a 2.3:1 mixture of diketopiperazines cyclo-(D-propyl-L-leucyl) and cyclo-(L-prolyl-L-leucyl).These two species account for most of the leucine and proline in the final mixture after the tetrapeptide is no longer detectable.Only small amounts of prolylleucine can be detcected after 50 hours.It is suggested that the above tetrapeptide undergoes internal aminolysis.Leucine in the tetrapeptide glycyl-L-leucylglycylglycine racemizes three times faster than in L-propyl-L-leucylglycylglycine.This demonstrates that an amino acid residue in a peptide chain does have an effect upon the rate of epimerization of a neighbouring peptide residue.A discussion of the geochemical implications of the results is included.