1257849-07-2

Basic information

• Product Name: Fmoc-5-chloro-L-tryptophan
• Synonyms: Fmoc-5-chloro-L-tryptophan;Fmoc-Trp(5-Cl)-OH;5-Chloro-N-Fmoc-L-tryptophan;(9H-Fluoren-9-yl)MethOxy]Carbonyl Trp(5-Cl)-OH;Fmoc-L-5-ChloroTryptophan
• CAS NO: 1257849-07-2
• Molecular Formula: C26H21ClN2O4
• Molecular Weight: 460.90894
• Mol File: 1257849-07-2.mol
• Article Data: 2

Chemical Properties

• Boiling Point: 732.6±60.0 °C(Predicted)
• Appearance: /
• Density: 1.406±0.06 g/cm3(Predicted)
• Storage Temp.: 2-8°C
• PKA: 3.71±0.10(Predicted)
• CAS DataBase Reference: Fmoc-5-chloro-L-tryptophan(CAS DataBase Reference)
• NIST Chemistry Reference: Fmoc-5-chloro-L-tryptophan(1257849-07-2)
• EPA Substance Registry System: Fmoc-5-chloro-L-tryptophan(1257849-07-2)

Safety Data

• Hazardous Substances Data: 1257849-07-2(Hazardous Substances Data)

Usage

General Description

Fmoc-5-chloro-L-tryptophan is a chemical compound commonly used in the synthesis of peptides and proteins. It is a derivative of the amino acid tryptophan, with a 5-chloro substitution. The Fmoc group is a protecting group commonly used in peptide synthesis to protect the amine group of amino acids. Fmoc-5-chloro-L-tryptophan is often used in solid-phase peptide synthesis due to its ability to selectively react with other amino acids and form peptide bonds. Due to its specific properties, this chemical is widely utilized in the pharmaceutical and biotechnology industries for the production of peptide-based drugs and research.

Upstream product

• 17422-32-1 5-chloro-1H-indole 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 827-01-0 5-chloro-1H-indole-3-carboxaldehyde 

Relevant articles and documents

Structure-Based Design of Melanocortin 4 Receptor Ligands Based on the SHU-9119-hMC4R Cocrystal Structure ?

The melanocortin receptors (MC1R-MC5R) belong to class A G-protein-coupled receptors (GPCRs) and are known to have receptor-specific roles in normal and diseased states. Selectivity for MC4R is of particular interest due to its involvement in various metabolic disorders, including obesity, feeding regulation, and sexual dysfunctions. To further improve the potency and selectivity of MC4R (ant)agonist peptide ligands, we designed and synthesized a series of cyclic peptides based on the recent crystal structure of MC4R in complex with the well-characterized antagonist SHU-9119 (Ac-Nle4-c[Asp5-His6-DNal(2′)7-Arg8-Trp9-Lys10]-NH2). These analogues were pharmacologically characterized in vitro, giving key insights into exploiting binding site subpockets to deliver more selective ligands. More specifically, the side chains of the Nle4, DNal(2′)7, and Trp9 residues in SHU-9119, as well as the amide linkage between the Asp5 and Lys10 side chains, were found to represent structural features engaging a hMC4R/hMC3R selectivity switch.