《Cu-Catalyzed site-selective C(sp2)-H radical trifluoromethylation of tryptophan-containing peptides》 was written by Guerrero, Itziar; Correa, Arkaitz. Computed Properties of C12H15ClN2O2This research focused ontryptophan peptide radical trifluoromethylation copper catalyst chirality; crystal structure tryptophan trifluoromethylation reaction mechanism solvent effect. The article conveys some information:
Site-selective functionalization of C-H bonds within a peptide framework poses a challenging task of paramount synthetic relevance. Herein, we report an operationally simple C(sp2)-H trifluoromethylation of tryptophan (Trp)-containing peptides. This fluorination technique is characterized by its chirality preservation, tolerance of functional groups, and scalability and exhibits chemoselectivity for Trp residues over other amino acid and heterocyclic units. As a result, it represents a sustainable tool toward the late-stage peptide modification and protein engineering.H-Trp-OMe.HCl(cas: 7524-52-9Computed Properties of C12H15ClN2O2) was used in this study.
H-Trp-OMe.HCl(cas:7524-52-9) is one of amino acid derivatives. Amino acid derivatives represent an important category of skin penetration promoters. These compounds possess hydrophobic chains attached to an amino acid headgroup via a biodegradable ester bond. Due to the amphiphilic nature of these derivatives, it is possible for them to enter into the SC lipid barrier and significantly disorganize skin membrane lipids.Computed Properties of C12H15ClN2O2
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