《C-H olefination of tryptophan residues in peptides: Control of residue selectivity and peptide-amino acid cross-linking》 was written by Terrey, Myles J.; Holmes, Ashley; Perry, Carole C.; Cross, Warren B.. Category: esters-buliding-blocksThis research focused ontryptophan peptide synthesis olefination solvent effect; peptide amino acid cross linking residue selectivity; protective group peptide coupling. The article conveys some information:
There is high demand for new methods to modify peptides, for application in drug discovery and biomedicine. A C-H functionalization protocol for the olefination of tryptophan residues in peptides is described. The modification is successful for Trp residues at any position in the peptide, has broad scope in the styrene coupling partner, and offers opportunities for conjugating peptides with other biomols. For peptides containing both Trp and Phe, directing group manipulation enables full control of residue selectivity. In the experiment, the researchers used H-Trp-OMe.HCl(cas: 7524-52-9Category: esters-buliding-blocks)
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.Category: esters-buliding-blocks
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Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics