36077-41-5

Usage

Uses

Used in Pharmaceutical Industry:
H-LEU-ILE-OH is used as a pharmaceutical agent for its ghrelin release-modulating activity. This property makes it a potential candidate for the development of drugs targeting conditions related to ghrelin dysregulation.
Used in Cardiovascular Applications:
H-LEU-ILE-OH is used as a potential anti-hypertensive agent due to its ability to modulate blood pressure. This application could be beneficial in the development of treatments for hypertension and related cardiovascular conditions.

Upstream product

• 909874-75-5 N-(2-bromo-4-methyl-valeryl)-isoleucine 
• 42537-96-2 N-(N-benzyloxycarbonyl-L-leucyl)-L-isoleucine 
• 2577-46-0 L-isoleucine methyl ester 
• 76863-45-1 (S)-benzyl (1-azido-4-methyl-1-oxopentan-2-yl)carbamate 
• 2018-66-8 Z-Leu-OH 
• 1480-30-4 (S)-2-(2,2,2-trifluoroacetamido)-4-methylpentanoic acid 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 53613-22-2 (N-(tert-butoxycarbonyl)-L-leucinyl)-L-isoleucine methyl ester 
• 65057-75-2 tert-butoxycarbonyl-L-leucyl-L-isoleucine 
• 35661-60-0 Fmoc-Leu-OH 
• 71989-23-6 Fmoc-Ile-OH 
• 4817-98-5 Z-Leu-Ile-OMe 

Relevant academic research and scientific papers

Synthesis of L-leucyl-L-isoleucine and L-isoleucyl-L-leucine

New preparative procedures were developed applying tert-butoxycarbonyl or trifluoroacetyl protection of amino groups in the synthesis of L-leucyl-L-isoleucine and L-isoleucyl-L-leucine.

Champacyclin, a new cyclic octapeptide from Streptomyces strain C42 isolated from the Baltic Sea

New isolates of Streptomyces champavatii were isolated from marine sediments of the Gotland Deep (Baltic Sea), from the Urania Basin (Eastern Mediterranean), and from the Kiel Bight (Baltic Sea). The isolates produced several oligopeptidic secondary metabolites, including the new octapeptide champacyclin (1a) present in all three strains. Herein, we report on the isolation, structure elucidation and determination of the absolute stereochemistry of this isoleucine/leucine (Ile/Leu = Xle) rich cyclic octapeptide champacyclin (1a). As 2D nuclear magnetic resonance (NMR) spectroscopy could not fully resolve the structure of (1a), additional information on sequence and configuration of stereocenters were obtained by a combination of multi stage mass spectrometry (MSn) studies, amino acid analysis, partial hydrolysis and subsequent enantiomer analytics with gas chromatography positive chmical ionization/electron impact mass spectrometry (GC-PCI/EI-MS) supported by comparison to reference dipeptides. Proof of the head-to-tail cyclization of (1a) was accomplished by solid phase peptide synthesis (SPPS) compared to an alternatively side chain cyclized derivative (2). Champacyclin (1a) is likely synthesized by a non-ribosomal peptide synthetase (NRPS), because of high content of (D)-amino acids. The compound (1a) showed antimicrobial activity against the phytopathogen Erwinia amylovora causing the fire blight disease of certain plants.

DPP4 INHIBITOR AND PHARMACEUTICAL APPLICATION THEREOF

The present invention provides a Dpp4 inhibitor which comprises a leucine derivative of the following formula (1) or a methionine derivative of the following formula (2): wherein each R1 and R3 represents a hydrogen atom (H) and an L-amino acid residue; R2 represents a hydroxyl group (OH), alkoxy group having 1 to 6 carbon atoms, amino group (NH2), alkylamino group having 1 to 6 carbon atoms, glycine residue, β-alanine residue, L-amino acid (except for proline, alanine and phenylalanine) residue or L-amino-acid amide (except for proline amide, alanine amide and phenylalanine amide) residue; and R4 represents a hydroxyl group (OH), alkoxy group having 1 to 6 carbon atoms, amino group (NH2), alkylamino group having 1 to 6 carbon atoms, glycine residue, β-alanine residue, L-amino acid (except for proline and alanine) residue or L-amino-acid amide (except for proline amide and alanine amide) residue. These derivatives also act as autophagy regulators.