N‐Terminal Modification of Gly‐His‐Tagged Proteins with Azidogluconolactone

Site‐specific protein modifications are vital for biopharmaceutical drug development. Gluconoylation is a non‐enzymatic, post‐translational modification of N‐terminal HisTags. We report high‐yield, site‐selective in vitro α‐aminoacylation of peptides, glycoproteins, antibodies, and virus‐like partic...

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Vydané v:	Chembiochem : a European journal of chemical biology Ročník 22; číslo 22; s. 3199 - 3207
Hlavní autori:	Brune, Karl D., Liekniņa, Ilva, Sutov, Grigorij, Morris, Alexander R., Jovicevic, Dejana, Kalniņš, Gints, Kazāks, Andris, Kluga, Rihards, Kastaljana, Sabine, Zajakina, Anna, Jansons, Juris, Skrastiņa, Dace, Spunde, Karīna, Cohen, Alexander A., Bjorkman, Pamela J., Morris, Howard R., Suna, Edgars, Tārs, Kaspars
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	Weinheim Wiley Subscription Services, Inc 16.11.2021
Predmet:	Aminoacylation Antibodies Antigens Biopharmaceuticals click chemistry COVID-19 COVID-19 vaccines Drug development Esters Glycoproteins Glycosylation immunology nanoparticles Peptides protein modifications Proteins R&D Research & development Seroconversion Severe acute respiratory syndrome coronavirus 2 site-specific conjugation Viruses Yeast
ISSN:	1439-4227, 1439-7633, 1439-7633
On-line prístup:	Získať plný text
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