16652-75-8

Basic information

• Product Name: L-Isoleucine benzyl ester 4-toluenesulphonate
• Synonyms: L-ISOLEUCINE BENZYL ESTER 4-TOLUENESULFONATE SALT;L-ISOLEUCINE BENZYL ESTER MONOTOSYLATE;L-ISOLEUCINE BENZYL ESTER P-TOLUENESULFONATE;L-ISOLEUCINE BENZYL ESTER P-TOLUENESULFONATE SALT;L-ISOLEUCINE BENZYL ESTER P-TOSYLATE;L-ISOLEUCINE BENZYL ESTER TOSYLATE;ISOLEUCINE BENZYL ESTER TOSYLATE;ISOLEUCINE-OBZL P-TOSYLATE
• CAS NO: 16652-75-8
• Molecular Formula: C₇H₈O₃S*C₁₃H₁₉NO₂
• Molecular Weight: 393.5
• EINECS: 240-701-0
• Product Categories: Amino Acids
• Mol File: 16652-75-8.mol
• Article Data: 4

Chemical Properties

• Melting Point: 153-155 °C
• Boiling Point: 545.1 °C at 760 mmHg
• Flash Point: 283.4 °C
• Appearance: /
• Vapor Pressure: 1.03E-12mmHg at 25°C
• Storage Temp.: Store at RT.
• Solubility: DMSO (Slightly), Methanol (Slightly)
• CAS DataBase Reference: L-Isoleucine benzyl ester 4-toluenesulphonate(CAS DataBase Reference)
• NIST Chemistry Reference: L-Isoleucine benzyl ester 4-toluenesulphonate(16652-75-8)
• EPA Substance Registry System: L-Isoleucine benzyl ester 4-toluenesulphonate(16652-75-8)

Safety Data

• Hazardous Substances Data: 16652-75-8(Hazardous Substances Data)

Usage

Description

L-Isoleucine benzyl ester 4-toluenesulphonate is a white powder chemical compound that serves as a reagent in the synthesis of various pharmaceutical agents. It is particularly utilized in the preparation of novel 10-hydroxycamptothecin prodrugs for antitumor treatment and in the synthesis of proteasome inhibitors, such as cystargolides A & B.

Uses

Used in Pharmaceutical Industry:
L-Isoleucine benzyl ester 4-toluenesulphonate is used as a reagent for the preparation of 10-hydroxycamptothecin prodrugs, which are employed in antitumor treatment. These prodrugs are designed to improve the therapeutic efficacy and reduce the side effects associated with traditional chemotherapy.
Used in Synthesis of Proteasome Inhibitors:
L-Isoleucine benzyl ester 4-toluenesulphonate is used as a key intermediate in the synthesis of proteasome inhibitors, such as cystargolides A & B. Proteasome inhibitors are a class of drugs that target the proteasome, a cellular enzyme complex responsible for the degradation of proteins. These inhibitors have potential applications in the treatment of various diseases, including cancer and neurodegenerative disorders, by modulating the protein degradation process.

InChI:InChI=1/C13H19NO2.C7H8O3S/c1-3-10(2)12(14)13(15)16-9-11-7-5-4-6-8-11;1-6-2-4-7(5-3-6)11(8,9)10/h4-8,10,12H,3,9,14H2,1-2H3;2-5H,1H3,(H,8,9,10)/t10-,12-;/m0./s1

Upstream product

• 42406-72-4 L-isoleucine benzyl ester 
• 104-15-4 toluene-4-sulfonic acid 
• 73-32-5 L-isoleucine 
• 100-51-6 benzyl alcohol 

Downstream Products

• 75666-44-3 Boc-Ile₂-OBzl 
• 90236-07-0 Boc-Glu(OBzl)-Ile-OBzl 
• 87053-36-9 Boc-Phe-Ile-OBzl 
• 162457-44-5 Boc-MeAbu-Ile-OBzl 
• 96409-00-6 ester benzylique de la N-(chloro-2-ethyl)-N-nitrosocarbamyl-L-isoleucine 
• 162457-57-0 Boc-BzlAbu-Ile-OBzl 
• 357429-11-9 N-Boc-L-(O-benzyl)tyrosyl-L-isoleucine benzyl ester 
• 1185762-28-0 (N,N-dimethyl-L-leucinyl)-L-isoleucine benzyl ester 
• 103725-76-4 Boc-L-Pro-L-Ile-OBz 
• 162457-36-5 Boc-Abu-Ile-OBzl 
• 128708-23-6 (2S,3S)-2-(tert-Butoxycarbonylmethyl-amino)-3-methyl-pentanoic acid benzyl ester; compound with toluene-4-sulfonic acid 
• 98748-09-5 Nα-diethylphosphinoylisoleucine benzyl ester 

Relevant articles and documents

Mortiamides A-D, Cyclic Heptapeptides from a Novel Mortierella sp. Obtained from Frobisher Bay

Four new cyclic heptapeptides, mortiamides A-D (1-4), were obtained from a novel Mortierella sp. isolate obtained from marine sediment collected from the intertidal zone of Frobisher Bay, Nunavut, Canada. The structures of the compounds were elucidated by NMR spectroscopy and tandem mass spectrometry. The absolute configurations of the amino acids were determined using Marfey's method. Localization of l and d amino acids within each compound was ascertained by retention time comparison of the partial hydrosylate products of each compound to synthesized dipeptide standards using LC-HRMS. Compounds 1-4 did not exhibit any significant antimicrobial or cytotoxic activity.

Self-assembly of amylin(20-29) amide-bond derivatives into helical ribbons and peptide nanotubes rather than fibrils

Uncontrolled aggregation of proteins or polypeptides can be detrimental for normal cellular processes in healthy organisms. Proteins or polypeptides that form these amyloid deposits differ in their primary sequence but share a common structural motif: the (anti)parallel β sheet. A well-accepted approach for interfering with -sheet formation is the design of soluble β-sheet peptides to disrupt the hydrogen-bonding network; this ultimately leads to the disassembly of the aggregates or fibrils. Here, we describe the synthesis, spectroscopic analysis, and aggregation behavior, imaged by electron microscopy, of several backbone-modified amylin(20-29) derivatives. It was found that these amylin derivatives were not able to form fibrils and to some extent were able to inhibit fibril growth of native amylin(20-29). However, two of the amylin peptides were able to form large supramolecular assemblies, like helical ribbons and peptide nanotubes, in which β-sheet formation was clearly absent. This was quite unexpectedWiley-VCH since these peptides have been designed as soluble β-sheet breakers for disrupting the characteristic hydrogen-bonding network of (anti)parallel β sheets. The increased hydrophobicity and the presence of essential amino acid side chains in the newly designed amylin(20-29) derivatives were found to be the driving force for self-assembly into helical ribbons and peptide nanotubes. This example of controlled and desired peptide aggregation may be a strong impetus for research on bionanomaterials in which special shapes and assemblies are the focus of interest.