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Decoupling Physisorption from Chemisorption in Clickable Lipid Nanoparticles.

Taylor V Brysgel1, Elizabeth D Hood1, Aleksa Milosavljevic2

  • 1Department of Systems Pharmacology and Translational Therapeutics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.

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PubMed
Summary
This summary is machine-generated.

Click chemistry for antibody-lipid nanoparticle (LNP) conjugation creates artifacts due to hydrophobic interactions. This leads to inaccurate measurements, but covalent bonding ensures effective in vivo targeting.

Keywords:
Antibody ConjugationClick ChemistryDrug DeliveryLipid NanoparticlesNanomedicineTargeting

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Area of Science:

  • Bioconjugation Chemistry
  • Nanoparticle Drug Delivery
  • Surface Chemistry

Background:

  • Antibody conjugation is critical for targeted lipid nanoparticle (LNP) delivery systems.
  • Click chemistry is a common method for achieving antibody-LNP conjugation.
  • Accurate measurement of covalent antibody-LNP bonds is essential for reliable targeting.

Purpose of the Study:

  • To investigate artifacts in antibody-LNP conjugation measurements using click chemistry.
  • To elucidate the role of hydrophobic interactions in antibody binding to LNPs.
  • To establish reliable methods for quantifying covalent antibody-LNP conjugation.

Main Methods:

  • Utilized click chemistry with dibenzocyclooctyne (DBCO) linkers for antibody conjugation to LNPs.
  • Assessed antibody binding via chromatographic methods and plasma incubation stability.
  • Compared conjugation efficiency on hydrophobic LNPs versus less hydrophobic liposomes.
  • Evaluated the impact of substituting DBCO with bicyclononyne (BCN).

Main Results:

  • Dibenzocyclooctyne (DBCO) linker's hydrophobicity drives significant nonspecific antibody physisorption onto LNPs.
  • This physisorption leads to artificially high conjugation efficiencies measured by chromatography.
  • Physisorbed antibodies are displaced by plasma, while covalently bound antibodies remain attached for effective in vivo targeting.
  • Less hydrophobic liposomes show azide-dependent conjugation, and BCN reduces nonspecific binding.

Conclusions:

  • Hydrophobicity is a critical, previously unrecognized variable in antibody-LNP conjugation.
  • Current click chemistry methods can overestimate covalent antibody attachment to LNPs.
  • New standards are needed for accurate, reproducible quantification of targeted LNPs.