What does this research mean for the field?

Asparaginyl endopeptidase (AEP) ligases enable highly efficient, site-selective functionalization of large molecular assemblies like P22 virus-like particles under mild conditions. Novelty: ClaimNovelty.METHODOLOGICAL. Consensus alignment: ConsensusAlignment.NEUTRAL.

What question did this study set out to answer?

To establish an efficient, site-selective bioconjugation method for functionalizing assembled Salmonella Typhimurium bacteriophage P22 virus-like particles using an asparaginyl endopeptidase ligase.

September 6, 2026Bioconjugate ChemistryOpen Access

Selective and Efficient Functionalization of P22 Virus-Like Particles Using an Asparaginyl Ligase

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Authors

MHMaxim D. Harding MJMark A. Jackson KYKuok Yap

Discussion

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Overview

In vitro study reveals efficient functionalization of bacteriophage P22 virus-like particles via asparaginyl ligase, suggesting new routes for targeted nanocarrier design.

Key Points

To establish an efficient, site-selective bioconjugation method for functionalizing assembled Salmonella Typhimurium bacteriophage P22 virus-like particles using an asparaginyl endopeptidase ligase.
Appended a minimal recognition motif to the C-terminus of bacteriophage P22 coat proteins to enable ligation by an asparaginyl endopeptidase (AEP).
Conjugated peptides and protein domains under mild reaction conditions, including a one-pot dual-functionalization reaction with two targeting domains.
Evaluated the in vitro receptor-binding activity of the functionalized virus-like particles.
AEP ligase successfully catalyzed site-selective conjugation of peptides and proteins onto intact P22 VLPs under mild reaction conditions.
A one-pot reaction achieved simultaneous dual-functionalization by attaching two distinct therapeutic receptor-targeting domains in a single step.
Conjugated P22 VLPs retained structural integrity and exhibited targeted receptor-binding functionality in vitro.

Cite This Study

Harding et al. (2026) studied this question.

synapsesocial.com/papers/6a9d1db828139818eab2082d https://doi.org/10.1021/acs.bioconjchem.6c00356

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September 6, 2026Bioconjugate ChemistryOpen Access

Selective and Efficient Functionalization of P22 Virus-Like Particles Using an Asparaginyl Ligase

View Full Paper

Ask AI

Bookmark

Authors

MHMaxim D. Harding MJMark A. Jackson KYKuok Yap

Discussion

Member takes

Overview

In vitro study reveals efficient functionalization of bacteriophage P22 virus-like particles via asparaginyl ligase, suggesting new routes for targeted nanocarrier design.

Key Points

To establish an efficient, site-selective bioconjugation method for functionalizing assembled Salmonella Typhimurium bacteriophage P22 virus-like particles using an asparaginyl endopeptidase ligase.
Appended a minimal recognition motif to the C-terminus of bacteriophage P22 coat proteins to enable ligation by an asparaginyl endopeptidase (AEP).
Conjugated peptides and protein domains under mild reaction conditions, including a one-pot dual-functionalization reaction with two targeting domains.
Evaluated the in vitro receptor-binding activity of the functionalized virus-like particles.
AEP ligase successfully catalyzed site-selective conjugation of peptides and proteins onto intact P22 VLPs under mild reaction conditions.
A one-pot reaction achieved simultaneous dual-functionalization by attaching two distinct therapeutic receptor-targeting domains in a single step.
Conjugated P22 VLPs retained structural integrity and exhibited targeted receptor-binding functionality in vitro.

Cite This Study

Harding et al. (2026) studied this question.

synapsesocial.com/papers/6a9d1db828139818eab2082d https://doi.org/10.1021/acs.bioconjchem.6c00356

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