105888-45-7

Basic information

• Product Name: H-Gln-AMC
• Synonyms: H-Gln-AMC;H-Gln-AMC Hydrobromide salt
• CAS NO: 105888-45-7
• Molecular Formula: C₁₅H₁₇N₃O₄
• Molecular Weight: 303.31318
• Mol File: 105888-45-7.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• CAS DataBase Reference: H-Gln-AMC(CAS DataBase Reference)
• NIST Chemistry Reference: H-Gln-AMC(105888-45-7)
• EPA Substance Registry System: H-Gln-AMC(105888-45-7)

Safety Data

• Hazardous Substances Data: 105888-45-7(Hazardous Substances Data)

Usage

General Description

H-Gln-AMC is a synthetic substrate commonly used in biochemical assays to measure the activity of enzymes such as glutaminyl-peptide cyclotransferase (QPCT). It consists of the amino acid glutamine (Gln) linked to the fluorogenic molecule 7-amino-4-methylcoumarin (AMC). When H-Gln-AMC is cleaved by an enzyme, the fluorescent signal of AMC is released, allowing for the quantification of enzyme activity. This substrate is particularly useful for studying pathways involving glutamine metabolism, as well as for screening and profiling potential enzyme inhibitors.

Upstream product

• 13726-85-7 Boc-Gln-OH 
• 105888-43-5 tert-butyl (S)-(5-amino-1-((4-methyl-2-oxo-2H-chromen-7-yl)amino)-1,5-dioxopentan-2-yl)carbamate 
• 26093-31-2 7-amino-4-methylcoumarin. 

Relevant articles and documents

Targeting the Main Protease of SARS-CoV-2: From the Establishment of High Throughput Screening to the Design of Tailored Inhibitors

The main protease of SARS-CoV-2 (Mpro), the causative agent of COVID-19, constitutes a significant drug target. A new fluorogenic substrate was kinetically compared to an internally quenched fluorescent peptide and shown to be ideally suitable for high throughput screening with recombinantly expressed Mpro. Two classes of protease inhibitors, azanitriles and pyridyl esters, were identified, optimized and subjected to in-depth biochemical characterization. Tailored peptides equipped with the unique azanitrile warhead exhibited concomitant inhibition of Mpro and cathepsin L, a protease relevant for viral cell entry. Pyridyl indole esters were analyzed by a positional scanning. Our focused approach towards Mpro inhibitors proved to be superior to virtual screening. With two irreversible inhibitors, azanitrile 8 (kinac/Ki=37 500 m?1 s?1, Ki=24.0 nm) and pyridyl ester 17 (kinac/Ki=29 100 m?1 s?1, Ki=10.0 nm), promising drug candidates for further development have been discovered.