15891-49-3

Basic information

• Product Name: AC-NLE-OH
• Synonyms: [S,(-)]-2-(Acetylamino)hexanoic acid;(S)-2-acetamidohexanoic acid;N-Acetylnorleucine;Acetyl-L-norleucine≥ 99% (HPLC);N-ACETYL-L-2-AMINO-CAPROIC ACID;N-ACETYL-L-NORLEUCINE;AC-L-NHCH[CH3(CH2)3]-COOH;AC-NLE-OH
• CAS NO: 15891-49-3
• Molecular Formula: C₈H₁₅NO₃
• Molecular Weight: 173.21
• Product Categories: Amino Acids
• Mol File: 15891-49-3.mol

Chemical Properties

• Melting Point: 114-115.5℃ (water )
• Boiling Point: 378.3oC at 760 mmHg
• Flash Point: 182.6oC
• Appearance: /
• Density: 1.072g/cm3
• Vapor Pressure: 9.05E-07mmHg at 25°C
• Refractive Index: 1.46
• Storage Temp.: Store at 0-5°C
• PKA: 3.68±0.10(Predicted)
• CAS DataBase Reference: AC-NLE-OH(CAS DataBase Reference)
• NIST Chemistry Reference: AC-NLE-OH(15891-49-3)
• EPA Substance Registry System: AC-NLE-OH(15891-49-3)

Safety Data

• Hazardous Substances Data: 15891-49-3(Hazardous Substances Data)

Usage

Chemical Properties

White powder

InChI:InChI=1/C8H15NO3/c1-3-4-5-7(8(11)12)9-6(2)10/h7H,3-5H2,1-2H3,(H,9,10)(H,11,12)/t7-/m0/s1

Upstream product

• 327-57-1 L-Norleucine 
• 108-24-7 acetic anhydride 
• 56247-43-9 N-acetylnorleucine methyl ester 

Downstream Products

• 327-57-1 L-Norleucine 
• 448944-47-6 Ac-Nle-Ala-His-D-Phe-Arg-Trp-NH₂ 

Relevant articles and documents

General Access to Modified α-Amino Acids by Bioinspired Stereoselective γ-C?H Bond Lactonization

α-Amino acids represent a valuable class of natural products employed as building blocks in biological and chemical synthesis. Because of the limited number of natural amino acids available, and of their widespread application in proteomics, diagnosis, drug delivery and catalysis, there is an increasing demand for the development of procedures for the preparation of modified analogues. Herein, we show that the use of bioinspired manganese catalysts and H2O2 under mild conditions, provides access to modified α-amino acids via γ-C?H bond lactonization. The system can efficiently target 1°, 2° and 3° γ-C?H bonds of α-substituted and achiral α,α-disubstituted α-amino acids with outstanding site-selectivity, good to excellent diastereoselectivity and (where applicable) enantioselectivity. This methodology may be considered alternative to well-established organometallic procedures.

Structure-activity relationship studies of dipeptide-based hepsin inhibitors with Arg bioisosteres

Hepsin is a type II transmembrane serine protease (TTSP) associated with cell proliferation and overexpressed in several types of cancer including prostate cancer (PCa). Because of its significant role in cancer progression and metastasis, hepsin is an attractive protein as a potential therapeutic and diagnostic biomarker for PCa. Based on the reported Leu-Arg dipeptide-based hepsin inhibitors, we performed structural modification and determined in vitro hepsin- and matriptase-inhibitory activities. Comprehensive structure-activity relationship studies identified that the p-guanidinophenylalanine-based dipeptide analog 22a exhibited a strong hepsin-inhibitory activity (Ki = 50.5 nM) and 22-fold hepsin selectivity over matriptase. Compound 22a could be a prototype molecule for structural optimization of dipeptide-based hepsin inhibitors.

Pronase catalysed peptide syntheses

A mixture of proteases from Streptomyces griseus (pronase), displaying a very broad substrate tolerance in the hydrolysis of peptides, has been studied for the first time systematically regarding their substrate specificity in peptide synthesis. It is demonstrated that pronase can be employed successfully for the formation of dipeptides with yields up to 95%. Pronase has also been employed successfully as catalyst for the enzyme assisted synthesis of a hexapeptide.