Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5611
Title: Humanin Structural versatility and interaction with model cerebral cortex membranes
Authors: Pistolesi, S
Rossini, L
Ferro, ELISA MARIA PAOLA
Basosi, Riccardo 
Trabalzini, Lorenza 
Pogni, Rebecca 
Issue Date: 2009
Project: None 
Journal: BIOCHEMISTRY
Abstract: 
Humanin (HN) is a recently identified neuroprotective peptide able to inhibit neurotoxicityinduced by various insults which can be related to Alzheimer disease (AD) as well as to cell death induced byother stimuli. Previous CD and NMR studies demonstrated that HN adopts an unordered conformation inwater, a R-helix conformation in 30% TFE, and a β-sheet structure in PBS. Furthermore, other studies clearlyindicated HN as a secreted peptide, able to prevent neuronal cell death caused by amyloid β (Aβ) derivatives.Although Aβ was found to interact with neuronal membranes, currently there is not experimental evidenceunveiling HN interaction with membranes. In this paper a spin labeling technique coupled with electronparamagnetic resonance (EPR) and circular dichroism (CD) has been used to study the structure anddynamics ofHNin solution and for the first time in the presence of model cerebral cortex membranes (CCM).We have demonstrated that HN has a great tendency to aggregate even at low concentrations in watersolutions at different ionic strengths and monomerizes in the TFE apolar environment. We also showed thatHN slightly perturbs model CCM at the surface assuming a clear β-sheet conformation. In addition, HNincreases the fluidity of the bilayer core without penetrating into the membrane.
Description: 
35076
URI: http://hdl.handle.net/20.500.12779/5611
ISSN: 0006-2960
DOI: 10.1021/bi900187s
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