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Rapid Generation of Amyloid from Native Proteins In vitro
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IgG Conformer's Binding to Amyloidogenic Aggregates.

Monichan Phay1, Alfred T Welzel2, Angela D Williams3

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Summary

Pooled plasma antibodies (pAbs) show enhanced binding to amyloid aggregates, with higher molecular weight (HMW) species being more active than monomers. These findings suggest potential for inherent anti-amyloid therapies.

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Area of Science:

  • Immunology
  • Neuroscience
  • Biochemistry

Background:

  • Pooled plasma antibodies (pAbs) are utilized for amyloid diseases, targeting amyloidogenic proteins.
  • The conformation of pAbs influences their binding activity to amyloid aggregates.

Purpose of the Study:

  • To investigate the binding characteristics of different pooled plasma antibody (pAb) conformers to amyloidogenic aggregates.
  • To explore the role of non-conventional interactions and aggregate modulation in pAb activity.

Main Methods:

  • Comparative analysis of binding affinities of monomeric, dimeric, and high molecular weight (HMW) pAb species to amyloid-beta (Aβ) and transthyretin (TTR) aggregates.
  • Assessment of antibody-target interactions using aggregated and monomeric forms of antibodies.
  • Evaluation of binding in human sera and comparison with murine pAbs and monoclonal antibodies (mAbs).

Main Results:

  • Higher molecular weight (HMW) pAb aggregates exhibited significantly stronger binding (up to ~200-fold) to amyloidogenic aggregates compared to monomers.
  • Dimeric pAbs also showed enhanced binding (~7-fold) compared to monomers.
  • Non-conventional interactions (outside of Complementarity-Determining Regions) contributed to pAb binding.
  • Trace aggregates during sample processing modulated pAb activity.
  • Monoclonal antibodies (mAbs) also showed conformation-dependent binding but with lower saturation.

Conclusions:

  • Pooled plasma antibody (pAb) conformation, particularly HMW species, significantly enhances binding to amyloidogenic aggregates.
  • Non-CDR interactions play a role in pAb binding to amyloid targets.
  • The inherent anti-amyloid activity of IgGs warrants further investigation for therapeutic potential.