TY - JOUR
T1 - Immunomodulation of the human prion peptide 106-126 aggregation
AU - Hanan, E.
AU - Goren, O.
AU - Eshkenazy, M.
AU - Solomon, B.
N1 - Funding Information:
This work was supported by The Center for the Study of Emerging Diseases. We would like to thank Rela Koppel for her technical help.
PY - 2001
Y1 - 2001
N2 - 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.
AB - 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.
KW - Aggregation
KW - Immunomodulation
KW - Monoclonal antibody
KW - Neurotoxicity
KW - Prion peptide
UR - http://www.scopus.com/inward/record.url?scp=0034805840&partnerID=8YFLogxK
U2 - 10.1006/bbrc.2000.4097
DO - 10.1006/bbrc.2000.4097
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AN - SCOPUS:0034805840
SN - 0006-291X
VL - 280
SP - 115
EP - 120
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -