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Ovine colostrum nanopeptide affects amyloid beta aggregation
Authors:Maria Janusz  Miros?aw Woszczyna  Adriana Kubis  Teodor Gotszalk
Institution:a Department of Immunochemistry, Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, 12 R. Weigla, 53-114 Wroc?aw, Poland
b Micro- and Nanostructure Metrology Group, Faculty of Microsystem Electronics and Photonics, Wroc?aw University of Technology, 11/17 Janiszewskiego, 50-372 Wroc?aw, Poland
c Chemistry and Stereochemistry of Peptides and Proteins Research Group, Faculty of Chemistry, Wroc?aw University, 14 Joliot-Curie, 50-383 Wroc?aw, Poland
d Institute of Biochemistry and Molecular Biology, Wroc?aw University, 2 Tamka, 50-137 Wroc?aw, Poland
Abstract:A colostral proline-rich polypeptide complex (PRP) consisting of over 30 peptides shows beneficial effects in Alzheimer’s disease (AD) patients when administered in the form of sublinqual tablets called Colostrinin. The aim of the present studies was to investigate whether nanopeptide fragment of PRP (NP) - one of the PRP complex components can affect aggregation of amyloid β (Aβ1-42). The effect of NP on Aβ aggregation was studied using Thioflavin T (ThT) binding, atomic force microscopy, and analyzing circular dichroism spectra. Results presented suggest that NP can directly interact with amyloid beta, inhibit its aggregation and disrupt existing aggregates acting as a β sheet breaker and reduce toxicity induced by aggregated forms of Aβ.
Keywords:PRP  proline-rich polypeptide complex from ovine colostrum  NP  nanopeptide fragment of PRP  AD  Alzheimer&rsquo  s disease    amyloid β  ThT  Thioflavin T  CD  circular dichroism  AFM  atomic force microscopy
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