1445137-79-0

Basic information

• Product Name: 2-(benzyloxycarbonylamino)-2-methylhept-6-enoic acid
• CAS NO: 1445137-79-0
• Molecular Weight: 291.347
• Mol File: 1445137-79-0.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: 2-(benzyloxycarbonylamino)-2-methylhept-6-enoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: 2-(benzyloxycarbonylamino)-2-methylhept-6-enoic acid(1445137-79-0)
• EPA Substance Registry System: 2-(benzyloxycarbonylamino)-2-methylhept-6-enoic acid(1445137-79-0)

Safety Data

• Hazardous Substances Data: 1445137-79-0(Hazardous Substances Data)

Usage

General Description

2-(benzyloxycarbonylamino)-2-methylhept-6-enoic acid is a chemical compound that belongs to the class of carboxylic acids. It is a derivative of 2-methylhept-6-enoic acid with a benzyloxy carbonyl group attached to the amino group. 2-(benzyloxycarbonylamino)-2-methylhept-6-enoic acid is commonly used in organic synthesis as a reagent for the protection of amino groups in peptide and protein chemistry. It is also used as a building block for the synthesis of complex molecules and pharmaceuticals. 2-(benzyloxycarbonylamino)-2-methylhept-6-enoic acid has potential applications in the field of medicinal chemistry and drug development.

Downstream Products

• 288617-73-2 (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-2-methylhept-6-enoic acid 

Relevant articles and documents

Design of cell-permeable stapled peptides as HIV-1 integrase inhibitors

HIV-1 integrase (IN) catalyzes the integration of viral DNA into the host genome, involving several interactions with the viral and cellular proteins. We have previously identified peptide IN inhibitors derived from the α-helical regions along the dimeric interface of HIV-1 IN. Herein, we show that appropriate hydrocarbon stapling of these peptides to stabilize their helical structure remarkably improves the cell permeability, thus allowing inhibition of the HIV-1 replication in cell culture. Furthermore, the stabilized peptides inhibit the interaction of IN with the cellular cofactor LEDGF/p75. Cellular uptake of the stapled peptide was confirmed in four different cell lines using a fluorescein-labeled analogue. Given their enhanced potency and cell permeability, these stapled peptides can serve as not only lead IN inhibitors but also prototypical biochemical probes or nanoneedles for the elucidation of HIV-1 IN dimerization and host cofactor interactions within their native cellular environment.