Janusz Maria, Woszczyna Mirosław, Lisowski Marek, Kubis Adriana, Macała Józefa, Gotszalk Teodor, Lisowski Józef
Department of Immunochemistry, Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław, Poland.
FEBS Lett. 2009 Jan 5;583(1):190-6. doi: 10.1016/j.febslet.2008.11.053. Epub 2008 Dec 10.
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 beta (Abeta1-42). The effect of NP on Abeta 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 beta sheet breaker and reduce toxicity induced by aggregated forms of Abeta.
一种由30多种肽组成的富含脯氨酸的初乳多肽复合物（PRP），以名为初乳素的舌下片剂形式给药时，对阿尔茨海默病（AD）患者显示出有益效果。本研究的目的是探究PRP复合物成分之一的PRP纳米肽片段（NP）是否会影响β淀粉样蛋白（Aβ1-42）的聚集。使用硫黄素T（ThT）结合、原子力显微镜以及分析圆二色光谱研究了NP对Aβ聚集的影响。呈现的结果表明，NP可直接与β淀粉样蛋白相互作用，抑制其聚集，破坏现有的聚集体，充当β折叠破坏剂，并降低由聚集形式的Aβ诱导的毒性。
