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The Evolution of SNAP-Tag Labels.
Dreyer, Rudolf; Pfukwa, Rueben; Barth, Stefan; Hunter, Roger; Klumperman, Bert.
Afiliação
  • Dreyer R; Stellenbosch University, Department of Chemistry and Polymer Science, Private Bag X1, Matieland 7602, South Africa.
  • Pfukwa R; Stellenbosch University, Department of Chemistry and Polymer Science, Private Bag X1, Matieland 7602, South Africa.
  • Barth S; Medical Biotechnology and Immunotherapy Research Unit, Institute of Infectious Disease and Molecular Medicine, Faculty of Health Sciences, University of Cape Town, Observatory 7935, South Africa.
  • Hunter R; South African Research Chair in Cancer Biotechnology, Department of Integrative Biomedical Sciences, Faculty of Health Sciences, University of Cape Town, Observatory 7935, South Africa.
  • Klumperman B; Department of Chemistry, Faculty of Science, University of Cape Town, Rondebosch 7701, South Africa.
Biomacromolecules ; 24(2): 517-530, 2023 02 13.
Article em En | MEDLINE | ID: mdl-36607253
ABSTRACT
The conjugation of proteins with synthetic molecules can be conducted in many different ways. In this Perspective, we focus on tag-based techniques and specifically on the SNAP-tag technology. The SNAP-tag technology makes use of a fusion protein between a protein of interest and an enzyme tag that enables the actual conjugation reaction. The SNAP-tag is based on the O6-alkylguanine-DNA alkyltransferase (AGT) enzyme and is optimized to react selectively with O6-benzylguanine (BG) substrates. BG-containing dye derivatives have frequently been used to introduce a fluorescent tag to a specific protein. We believe that the site-specific conjugation of polymers to proteins can significantly benefit from the SNAP-tag technology. Especially, polymers synthesized via reversible deactivation radical polymerization allow for the facile introduction of a BG end group to enable SNAP-tag conjugation.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas / O(6)-Metilguanina-DNA Metiltransferase Idioma: En Revista: Biomacromolecules Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2023 Tipo de documento: Article País de afiliação: África do Sul

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas / O(6)-Metilguanina-DNA Metiltransferase Idioma: En Revista: Biomacromolecules Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2023 Tipo de documento: Article País de afiliação: África do Sul