Abstract：
:Alzheimer's disease is a growing concern in the context of the increasing lifespan of the populations. The work presented here is part of the fight against this threat. It supports a therapeutic approach to reduce the incidence of Alzheimer's disease, taking advantage of the specific binding of several domains of Netrin-1 to the β-amyloid precursor protein. This basic knowledge shall then be used to predict, design or characterize lead compounds that may in turn inhibit/delay Alzheimer's disease's progression, extending the therapeutic offer of the other leads already being investigated in this line. The present work is focused on the interaction of the various portions of APP with the three domains of Netrin-1, the so-called LamNT, EGF-like and NTR domains respectively. It reveals in detail which portions of APP and Netrin-1 are specifically involved in these interactions, using ELISA technique in combination with protein-protein binding simulations. So far unsuspected interaction sites located in Netrin-1 EGF-like and NTR domains open possibilities for new therapeutic approaches in which these sites will be specifically targeted.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Borel F,Marzocca F,Delcros JG,Rama N,Mehlen P,Ferrer JLdoi
10.1016/j.bbrc.2017.05.056subject
Has Abstractpub_date
2017-07-01 00:00:00pages
466-470issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(17)30918-Xjournal_volume
488pub_type
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