92645-20-0Relevant articles and documents
Backbone amide linker (BAL) strategy for N(α)-9- fluorenylmethoxycarbonyl (Fmoc) solid-phase synthesis of unprotected peptide p-nitroanilides and thioesters
Alsina, Jordi,Yokum, T. Scott,Albericio, Fernando,Barany, George
, p. 8761 - 8769 (1999)
A novel and general backbone amide linker (BAL) strategy has been devised for preparation of C-terminal modified peptides containing hindered, unreactive, and/or sensitive moieties, in concert with N(α)-9- fluorenylmethoxycarbonyl (Fmoc) solid-phase synthesis protocols. This strategy comprises (i) start of peptide synthesis by anchoring the penultimate residue, with its carboxyl group orthogonally protected, through the backbone nitrogen, (ii) continuation with standard protocols for peptide chain elongation in the C→N direction, (iii) selective orthogonal removal of the carboxyl protecting group, (iv) solid-phase activation of the pendant carboxyl and coupling with the desired C-terminal residue, and (v) final cleavage/deprotection to release the free peptide product into solution. To illustrate this approach, several model peptide p-nitroanilides and thioesters have been prepared in excellent yields and purifies, with minimal racemization. Such compounds are very difficult to prepare by standard Fmoc chemistry, including the BAL strategy as originally envisaged.
Application of dehydroalanine as a building block for the synthesis of selenocysteine-containing peptides
Reddy, Kishorkumar M.,Mugesh, Govindasamy
, p. 34 - 43 (2019/01/16)
Selenocysteine (Sec), the 21st proteinogenic amino acid, is inserted co-translationally into number of natural proteins. It is coded by a dual function stop codon UGA (opal). It is a redox active amino acid found at the active sites of several
Visible-Light-Mediated Selective Arylation of Cysteine in Batch and Flow
Bottecchia, Cecilia,Rubens, Maarten,Gunnoo, Smita B.,Hessel, Volker,Madder, Annemieke,No?l, Timothy
supporting information, p. 12702 - 12707 (2017/09/08)
A mild visible-light-mediated strategy for cysteine arylation is presented. The method relies on the use of eosin Y as a metal-free photocatalyst and aryldiazonium salts as arylating agents. The reaction can be significantly accelerated in a microflow reactor, whilst allowing the in situ formation of the required diazonium salts. The batch and flow protocol described herein can be applied to obtain a broad series of arylated cysteine derivatives and arylated cysteine-containing dipeptides. Moreover, the method was applied to the chemoselective arylation of a model peptide in biocompatible reaction conditions (room temperature, phosphate-buffered saline (PBS) buffer) within a short reaction time.
