Immunomodulation of the human prion peptide 106-126 aggregation

E. Hanan, O. Goren, M. Eshkenazy, B. Solomon*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Site-directed monoclonal antibodies (mAbs) may interact with their antigens, leading to stabilization, refolding, and suppression of aggregation. In the following study, we show that mAbs raised against the peptide 106-126 of human prion protein (PrP 106-126) modulate the conformational changes occurring in the peptide exposed to aggregation conditions. MAbs 3-11 and 2-40 prevent PrP 106-126's fibrillar aggregation, disaggregates already formed aggregates, and inhibits the peptide's neurotoxic effect on the PC12 cells system, while mAb 3F4 has no protective effect. We suggest that there are key positions within the PrP 106-126 molecule where unfolding is initiated and their locking with specific antibodies may maintain the prion peptide native structure, reverse the aggregated peptide conformation, and lead to rearrangements involved in the essential feature of prion diseases.

Original languageEnglish
Pages (from-to)115-120
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume280
Issue number1
DOIs
StatePublished - 2001

Funding

FundersFunder number
Center for the Study of Emerging Diseases

    Keywords

    • Aggregation
    • Immunomodulation
    • Monoclonal antibody
    • Neurotoxicity
    • Prion peptide

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