Author(s): Zou P, Ding Y, Sha Y, Hu B, Nie S
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Abstract Humanin peptides (including HN, HNG and other mutants) were reported previously that antagonize neurotoxicity caused by various familial Alzheimer's disease (FAD) genes and Abeta derivatives. Herein, we describe the aggregation dynamics and the representative morphological characteristics of Abeta(1-40) after different time of addition humanin peptides, which revealed that (a) the interactions of both HN and HNG with Abeta(1-40) induced quick and significant increase of light-scattering intensity, and (b) HNG also caused obvious morphological alteration from fibrillary to amorphous. In the meantime, the experiments also revealed that the interaction of HNG with Abeta(1-40) could decrease Abeta(1-40)-induced calcium rise, an initial event accompanying Abeta(1-40)-induced apoptosis of cultured neurons. Our results indicate that HNG can protect neurons by altering Abeta(1-40) morphology.
This article was published in Peptides
and referenced in Journal of Cell Science & Therapy