Semisynthese eines homogenen Glycoprotein‐Enzyms: Ribonuclease C (Teil 1)

Abstract

Sieben auf einen Streich: Durch die effiziente Bildung von gemischten Disulfiden an dem thiolreichen Fusionsprotein A konnte nach Inteinabspaltung das Cys‐Fragment B mit sieben oxidationsgeschützten Cysteinen erhalten werden. Die native chemische Ligation von B mit synthetischen Glycopeptidthioestern ergibt Glycoproteine.

Semisynthesis of a Homogeneous Glycoprotein Enzyme: Ribonuclease C: Part 2

“…[11,12] The currently used methodology for the synthesis of N-glycoproteins comprises solid-phase glycopeptide synthesis, [13,14] the use of transglycosidases [15] or enzymatic remodeling, [16] the use of engineered cell lines, [17,18] and in particular the application of chemoselective ligation methods. [19][20][21] In the preceding Communication [22] we demonstrated that active RNase A can be obtained by expressed chemical ligation using a recombinant RNase segment that was chemically stabilized by transformation of its seven cysteines into mixed disulfides. We have taken this approach further to the synthesis of a single glycoform of bovine RNase carrying a biantennary complextype nonasaccharide (RNase C [23] ) by sequential [21,24] native chemical ligations (Scheme 1).…”

Transcriptome and gene expression analysis ofRhynchophorus ferrugineus(Coleoptera: Curculionidae) during developmental stages

“…Related research shows that R. ferrugineus is rich in phospholipids (2.6-9.3 g/100 g lipid) (Khanittha, Manat & Worawan, 2020). Moreover, the average protein content of edible insects is 10%-25% of fresh weight or 35%-60% of dry weight (Melo et al, 2011;Schlüter et al, 2016), even higher than the protein content of grains, lentils and soybeans (Bukkens, 1997). In fact, the dietary protein derived from insects is close to 50%, which is more market value than other proteins (Dobermann, Swift & Field, 2017).…”

The Linear Assembly of a Pure Glycoenzyme

“…[23] In a recent issue of Angewandte Chemie, two back-to-back papers by the Unverzagt group described progress in a powerful synthesis of a single glycoform of an enzyme. [40,41] They chose an excellent model system with which to demonstrate these strategic principles. Ribonuclease (RNase) is a 124-residue protein that has been an archetype of glycoprotein function by virtue of its single N-glycosylation site at Asn34.…”