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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Cagnotto, Alfredo Cantù, Laura Del Favero, Elena Salmona, Mario Stoilova, Tatiana Morbin, Michela Messa, Massimo Tagliavini, Fabrizio Colombo, Laura Rossi, Alessandro Di Fede, Giuseppe |
| Description | Author Affiliation: Messa M ( From the Department of Molecular Biochemistry and Pharmacology, IRCCS-Istituto di Ricerche Farmacologiche Mario Negri, Via La Masa 19, 20156, Milan, Italy.); Colombo L ( From the Department of Molecular Biochemistry and Pharmacology, IRCCS-Istituto di Ricerche Farmacologiche Mario Negri, Via La Masa 19, 20156, Milan, Italy.); del Favero E ( Department of Medical Biotechnology and Translational Medicine, University of Milan, V.le F.lli Cervi 93, 20090 Segrate, Italy, and.); Cantù L ( Department of Medical Biotechnology and Translational Medicine, University of Milan, V.le F.lli Cervi 93, 20090 Segrate, Italy, and.); Stoilova T ( From the Department of Molecular Biochemistry and Pharmacology, IRCCS-Istituto di Ricerche Farmacologiche Mario Negri, Via La Masa 19, 20156, Milan, Italy.); Cagnotto A ( From the Department of Molecular Biochemistry and Pharmacology, IRCCS-Istituto di Ricerche Farmacologiche Mario Negri, Via La Masa 19, 20156, Milan, Italy.); Rossi A ( From the Department of Molecular Biochemistry and Pharmacology, IRCCS-Istituto di Ricerche Farmacologiche Mario Negri, Via La Masa 19, 20156, Milan, Italy.); Morbin M ( Neurology V and Neuropathology, IRCCS Foundation 'Carlo Besta' Neurological Institute, Via Celoria 11, 20133 Milan, Italy.); Di Fede G ( Neurology V and Neuropathology, IRCCS Foundation 'Carlo Besta' Neurological Institute, Via Celoria 11, 20133 Milan, Italy.); Tagliavini F ( Neurology V and Neuropathology, IRCCS Foundation 'Carlo Besta' Neurological Institute, Via Celoria 11, 20133 Milan, Italy.); Salmona M ( From the Department of Molecular Biochemistry and Pharmacology, IRCCS-Istituto di Ricerche Farmacologiche Mario Negri, Via La Masa 19, 20156, Milan, Italy, mario.salmona@marionegri.it.) |
| Abstract | We recently reported a novel Aß precursor protein mutation (A673V), corresponding to position 2 of Aß1-42 peptides (Aß1-42A2V), that caused an early onset AD-type dementia in a homozygous individual. The heterozygous relatives were not affected as an indication of autosomal recessive inheritance of this mutation. We investigated the folding kinetics of native unfolded Aß1-42A2V in comparison with the wild type sequence (Aß1-42WT) and the equimolar solution of both peptides (Aß1-42MIX) to characterize the oligomers that are produced in the early phases. We carried out the structural characterization of the three preparations using electron and atomic force microscopy, fluorescence emission, and x-ray diffraction and described the soluble oligomer formation kinetics by laser light scattering. The mutation promoted a peculiar pathway of oligomerization, forming a connected system similar to a polymer network with hydrophobic residues on the external surface. Aß1-42MIX generated assemblies very similar to those produced by Aß1-42WT, albeit with slower kinetics due to the difficulties of Aß1-42WT and Aß1-42A2V peptides in building up of stable intermolecular interaction. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 35 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-08-29 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Amyloid Beta-Peptides Genetics Mutation Peptide Fragments Chemistry Circular Dichroism Kinetics Microscopy, Atomic Force Polymerization Protein Folding Scattering, Small Angle Spectrometry, Fluorescence X-Ray Diffraction Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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