Self‐Immolative Nanobody‐Cysteine Residue Modification for Controlled Immunodrug Delivery
Abstract: Applications of antibody‐drug conjugates are rapidly growing, however, arduous fabrication of antibodies and impairment of highly potent drugs by covalent fixation to the protein is urging for alternatives to these conventional strategies. Here, a procedure on genetically engineered single domain antibodies, so‐called nanobodies, is demonstrated for their site‐specific reversible bioconjugation using self‐immolative linkers (SILs). Straight‐forward fluorescent labelling at their C‐terminal cysteine can be reversed under reductive conditions due to its disulfide‐containing SIL. Flow cytometry and microscopy images demonstrate cellular uptake and confirm the integrity of the nanobodies’ biological affinity notwithstanding being modified. Following this strategy, a potent small molecular immunomodulator can be installed and its stimulatory effect on a cellular level is boosted in vitro compared to non‐degradable alternatives. Furthermore, this protocol is extended to further therapeutically relevant representatives of nanobodies, underlining the versatility of this reversible reductive‐responsive bioconjugation for a broad field of applications.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Self‐Immolative Nanobody‐Cysteine Residue Modification for Controlled Immunodrug Delivery ; day:18 ; month:07 ; year:2023 ; extent:8
Advanced therapeutics ; (18.07.2023) (gesamt 8)
- Creator
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Scherger, Maximilian
Pilger, Yannick A.
Stickdorn, Judith
Komforth, Patric
Schmitt, Sascha
Arnouk, Sana M.
Lebegge, Els
Koynov, Kaloian
Räder, Hans‐Joachim
Van Ginderachter, Jo A.
Nuhn, Lutz
- DOI
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10.1002/adtp.202300076
- URN
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urn:nbn:de:101:1-2023071815183811372100
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:55 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Scherger, Maximilian
- Pilger, Yannick A.
- Stickdorn, Judith
- Komforth, Patric
- Schmitt, Sascha
- Arnouk, Sana M.
- Lebegge, Els
- Koynov, Kaloian
- Räder, Hans‐Joachim
- Van Ginderachter, Jo A.
- Nuhn, Lutz
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A cysteine residue within the kinase domain of Zap70 regulates Lck activity and proximal TCR signaling
Conserved active site cysteine residue of archaeal THI4 homolog is essential for thiamine biosynthesis in Haloferax volcanii
Transdermal Administration of Nanobody Molecules using Hydrogel‐Forming Microarray Patch Technology: A Unique Delivery Approach
Cysteine‐Selective Modification of Peptides and Proteins via Desulfurative C−C Bond Formation
Reactivity‐Tunable Fluorescent Platform for Selective and Biocompatible Modification of Cysteine or Lysine
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Mechanisms and engineering of nanobody thermoresistance
Die Entwicklung von Nanobody-funktionalisierten Goldoberflächen
Quaternization of Vinyl/Alkynyl Pyridine Enables Ultrafast Cysteine‐Selective Protein Modification and Charge Modulation
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Conformational instability of human prion protein upon residue modification: a molecular dynamics simulation study
Nanobody-Displaying Flagellar Nanotubes
A cysteine residue within the kinase domain of Zap70 regulates Lck activity and proximal TCR signaling
Conserved active site cysteine residue of archaeal THI4 homolog is essential for thiamine biosynthesis in Haloferax volcanii
Transdermal Administration of Nanobody Molecules using Hydrogel‐Forming Microarray Patch Technology: A Unique Delivery Approach
Cysteine‐Selective Modification of Peptides and Proteins via Desulfurative C−C Bond Formation
Reactivity‐Tunable Fluorescent Platform for Selective and Biocompatible Modification of Cysteine or Lysine
Engineering A‐type Dye‐Decolorizing Peroxidases by Modification of a Conserved Glutamate Residue
Mechanisms and engineering of nanobody thermoresistance
Die Entwicklung von Nanobody-funktionalisierten Goldoberflächen
Quaternization of Vinyl/Alkynyl Pyridine Enables Ultrafast Cysteine‐Selective Protein Modification and Charge Modulation
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