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Highly Selective Lysine Acylation in Proteins Using a Lys-His Tag Sequence.
Kofoed, Christian; Wu, Shunliang; Sørensen, Kasper K; Treiberg, Tuule; Arnsdorf, Johnny; Bjørn, Sara P; Jensen, Tanja L; Voldborg, Bjørn G; Thygesen, Mikkel B; Jensen, Knud J; Schoffelen, Sanne.
Afiliación
  • Kofoed C; Department of Chemistry, University of Copenhagen, Thorvaldsensvej 40, 1871, Frederiksberg, Denmark.
  • Wu S; Present address: Frick Chemistry Laboratories, Princeton University, 08544, New Jersey, USA.
  • Sørensen KK; Department of Chemistry, University of Copenhagen, Thorvaldsensvej 40, 1871, Frederiksberg, Denmark.
  • Treiberg T; Department of Chemistry, University of Copenhagen, Thorvaldsensvej 40, 1871, Frederiksberg, Denmark.
  • Arnsdorf J; Department of Chemistry, University of Copenhagen, Thorvaldsensvej 40, 1871, Frederiksberg, Denmark.
  • Bjørn SP; National Biologics Facility, Department of Biotechnology and Biomedicine, Technical University of Denmark, Building 220, Kemitorvet, 2800, Kgs. Lyngby, Denmark.
  • Jensen TL; National Biologics Facility, Department of Biotechnology and Biomedicine, Technical University of Denmark, Building 220, Kemitorvet, 2800, Kgs. Lyngby, Denmark.
  • Voldborg BG; The Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Building 220, Kemitorvet, 2800, Kgs. Lyngby, Denmark.
  • Thygesen MB; National Biologics Facility, Department of Biotechnology and Biomedicine, Technical University of Denmark, Building 220, Kemitorvet, 2800, Kgs. Lyngby, Denmark.
  • Jensen KJ; Department of Chemistry, University of Copenhagen, Thorvaldsensvej 40, 1871, Frederiksberg, Denmark.
  • Schoffelen S; Department of Chemistry, University of Copenhagen, Thorvaldsensvej 40, 1871, Frederiksberg, Denmark.
Chemistry ; 28(15): e202200147, 2022 Mar 10.
Article en En | MEDLINE | ID: mdl-35099088
Chemical modification of proteins has numerous applications, but it has been challenging to achieve the required high degree of selectivity on lysine amino groups. Recently, we described the highly selective acylation of proteins with an N-terminal Gly-His6 segment. This tag promoted acylation of the N-terminal Nα -amine resulting in stable conjugates. Herein, we report the peptide sequences Hisn -Lys-Hism , which we term Lys-His tags. In combination with simple acylating agents, they facilitate the acylation of the designated Lys Nϵ -amine under mild conditions and with high selectivity over native Lys residues. We show that the Lys-His tags, which are 7 to 10 amino acids in length and still act as conventional His tags, can be inserted in proteins at the C-terminus or in loops, thus providing high flexibility regarding the site of modification. Finally, the selective and efficient acylation of the therapeutic antibody Rituximab, pure or mixed with other proteins, demonstrates the scope of the Lys-His tag acylation method.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas / Lisina Idioma: En Revista: Chemistry Asunto de la revista: QUIMICA Año: 2022 Tipo del documento: Article País de afiliación: Dinamarca Pais de publicación: Alemania
Texto completo
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Imprimir
XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas / Lisina Idioma: En Revista: Chemistry Asunto de la revista: QUIMICA Año: 2022 Tipo del documento: Article País de afiliación: Dinamarca Pais de publicación: Alemania