22951-98-0

Basic information

• Product Name: H-ILE-PHE-OH
• Synonyms: L-ISOLEUCYL-L-PHENYLALANINE;H-ILE-PHE-OH;L-ILE-L-PHE;ILE-PHE
• CAS NO: 22951-98-0
• Molecular Formula: C₁₅H₂₂N₂O₃
• Molecular Weight: 278.35
• Mol File: 22951-98-0.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 501.2±50.0 °C(Predicted)
• Appearance: /
• Density: 1.144±0.06 g/cm3(Predicted)
• Storage Temp.: -15°C
• Solubility: Methanol (Slightly, Sonicated)
• PKA: 3.41±0.10(Predicted)
• CAS DataBase Reference: H-ILE-PHE-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-ILE-PHE-OH(22951-98-0)
• EPA Substance Registry System: H-ILE-PHE-OH(22951-98-0)

Safety Data

• Hazardous Substances Data: 22951-98-0(Hazardous Substances Data)

Usage

General Description

H-ILE-PHE-OH is a chemical compound derived from the amino acids isoleucine and phenylalanine. It is a peptide with a carboxylic acid group at one end. H-ILE-PHE-OH may have potential applications in pharmaceuticals, as it contains amino acids that are important for the synthesis of proteins and regulation of metabolism. Additionally, it may have bioactive properties due to its peptide structure, making it a potential candidate for the development of drugs or biologically active compounds. Further research is needed to fully understand the potential uses and effects of H-ILE-PHE-OH.

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

Relevant articles and documents

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.

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