22951-98-0

Usage

Uses

Used in Pharmaceutical Industry:
H-ILE-PHE-OH is used as a potential pharmaceutical compound for its role in protein synthesis and metabolic regulation, as well as for its possible bioactive properties that could contribute to the development of new drugs or biologically active compounds. The specific applications and effects of H-ILE-PHE-OH in this industry are still under investigation and require further research to be fully understood and harnessed.

Upstream product

• 85310-51-6 N-(benzyloxycarbonyl)isoleucylphenylalanine benzyl ester 
• 35661-40-6 N-Fmoc L-Phe 
• 71989-23-6 Fmoc-Ile-OH 

Downstream Products

• 90315-68-7 N-(benzyloxycarbonyl)valylisoleucylphenylalanine 
• 54793-60-1 H-(S)-Ile-(S)-Phe-OCH₃ 
• 90315-71-2 N-(benzyloxycarbonyl)valylisoleucylphenylalanylprolylprolylglycyl-N^G-nitroarginine benzyl ester 
• 90315-69-8 N-(benzyloxycarbonyl)valylisoleucylphenylalanylprolylprolylglycine benzyl ester 
• 90315-70-1 N-(benzyloxycarbonyl)valylisoleucylphenylalanylprolylprolylglycine 
• 13254-07-4 N-Benzyloxycarbonyl-L-isoleucyl-L-phenylalanin 

Relevant academic research and scientific papers

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.

Covalent capture purification of polypeptides after SPPS via a linker removable under very mild conditions

The covalent purification of polypeptides possessing an N-terminal cysteine or threonine residue via formation of a thiazolidine or oxazolidine with an aldehyde-functionalized-resin has been successfully demonstrated. To extend the applicability of this approach to any possible N-terminal residue, a special linker derived from (S)-4-amino-2-hydroxy-butyric acid was incorporated into peptidyl-resin. This linker represents the connecting point between the capture unit (cysteine) useful for the isolation of the desired polypeptide and the desired N-terminus. The target polypeptide was recovered by periodate oxidation, which cleaved the covalent bond between the linker and the last residue of polypeptide under very mild conditions.

STUDIES OF BITTER PEPTIDES FROM CASEIN HYDROLYZATE - VII. BITTERNESS OF THE RETRO-BPIa (VAL-ILE-PHE-PRO-PRO-GLY-ARG) AND ITS FRAGMENTS.

To explain the bitter taste exhibited by BPIa (Arg-Gly-Pro-Pro-Phe-Ile-Val) which was isolated from casein hydrolyzate, the authors propose the following requirement: its characteristic spatial structure: the basic moiety in the N-terminal and the hydroph