1320358-56-2Relevant academic research and scientific papers
Accelerated Protein Synthesis via One-Pot Ligation-Deselenization Chemistry
Mitchell, Nicholas J.,Sayers, Jessica,Kulkarni, Sameer S.,Clayton, Daniel,Goldys, Anna M.,Ripoll-Rozada, Jorge,Barbosa Pereira, Pedro José,Chan, Bun,Radom, Leo,Payne, Richard J.
supporting information, p. 703 - 715 (2017/05/15)
Peptide ligation chemistry has revolutionized protein science by facilitating access to synthetic proteins. Here, we describe the development of additive-free ligation-deselenization chemistry at β-selenoaspartate and γ-selenoglutamate that enables the generation of native polypeptide products on unprecedented timescales. The deselenization step is chemoselective in the presence of unprotected selenocysteine, which is highlighted in the synthesis of selenoprotein K. The power of the methodology is also showcased through the synthesis of three tick-derived thrombin-inhibiting proteins, each of which were assembled, purified, and isolated for biological assays within a few hours. The methodology described here should serve as a powerful means of accessing synthetic proteins, including therapeutic leads, in the future.
One-pot peptide ligation-desulfurization at glutamate
Cergol, Katie M.,Thompson, Robert E.,Malins, Lara R.,Turner, Peter,Payne, Richard J.
supporting information, p. 290 - 293 (2014/01/23)
An efficient methodology for ligation at glutamate (Glu) is described. A γ-thiol-Glu building block was accessed in only three steps from protected glutamic acid and could be incorporated at the N-terminus of peptides. The application of these peptides in one-pot ligation-desulfurization chemistry is demonstrated with a range of peptide thioesters, and the utility of this methodology is highlighted through the synthesis of the osteoporosis peptide drug teriparatide (Forteo).
Peptide ligations accelerated by N-terminal aspartate and glutamate residues
Thomas, Gemma L.,Hsieh, Yves S. Y.,Chun, Candy K. Y.,Cai, Zheng-Li,Reimers, Jeffrey R.,Payne, Richard J.
supporting information; experimental part, p. 4770 - 4773 (2011/11/12)
A novel application of intramolecular base catalysis confers enhanced reaction rates for aminolysis ligations between peptide thioesters and peptides bearing N-terminal aspartate or glutamate residues. The broad scope of this process and its application i
