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The latest news about our therapeutic molecule AmyP53 !

website amypore.com

 

 

 

Un roman scientifique de haut vol 

 

L'ADN perdu: le secret de la Vie dans l'Univers

Disponible sur Amazon  (bénéfices de l'auteur versés à une association d'aide aux enfants hospitalisés)

 déjà 120€ versés 

à Sourire à la Vie

 

 Hypothèse stupéfiante sur l'origine de la vie ! 

Je recommande +++ 

 

Informations

 

Les étudiants de la Licence Sciences de la Vie à l'Université d'Aix-Marseille (L3 Parcours PGF) rivalisent de talent pour fabriquer des vésicules prébiotiques en séance de Travaux Pratiques.

 

Voici une magnifique image de ces vésicules préparées avec seulement 3 composés issus de météorites :

 

de l'eau, de l'acide nonanoïque et du nonanol.

 

Travail d'Eva BARASTON, Sofiane BENHAMED et Sarah BRAHIMI (5/12/2023)

 

UE Origine de la Vie & Evolution Moléculaire

Observation au microscope optique

 

Expérience réalisée selon la méthode de David Deamer :

 

Self-assembled vesicles of monocarboxylic acids and alcohols: conditions for stability and for the encapsulation of biopolymers.

Apel CL, Deamer DW, Mautner MN.Biochim Biophys Acta. 2002 Feb 10;1559(1):1-9. 
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AmyP53 therapeutic innovation

for Alzheimer and Parkinson

 

Video explanation of AmyP53 technology.

© Christelle GOBET, a talented student in Neurobiology 

in english:

and in french:

 

Molecular modeling of amyloid pores (J. Fantini)

Amyloid plaques are no longer regarded as the pathogenic forms of Alzheimer's beta amyloid peptide (Abeta). Instead, small oligomers of amyloid proteins (Abeta and alpha-synuclein) that form Ca2+ permeable  channels (amyloid pores) are now  considered as the most neurotoxic species of amyloid proteins in neurodegenerative disorders. By disrupting Ca2+ homeostasis in brain cells, amyloid oligomers induce dramatic synaptic dysfunctions, impaired plasticity and neuronal degeneration. Hence, the oligomer  model has all but supplanted the classical amyloid cascade.

 

Our group demonstrated that amyloid pores are formed by a common mecanism that can be summarized in three steps: 1- binding of the amyloid protein to the plasma membrane of a brain cell through a primary interaction with a ganglioside (GM1 or GM3) followed by 2- cholesterol-assisted insertion and 3- oligomerization into a Ca2+ permeable pore (Di Scala et al., Sci Rep. 2016, 6: 28781).

 

Elucidating this universal mechanism allowed us to create the first inhibitor of amyloid pore formation, now called AmyP53, that is active against wild-type and mutant forms of the proteins involved in Alzheimer's and Parkinson's diseases. A full description of the anti-pore properties of this inhibitor has been published here. 

 

Disruptive technology

AmyP53 is not only one of the first molecules that target the oligomer cascade, it is the only one that  can block the formation of the neurotoxic oligomers in the plasma membrane of brain cells.

 

Therapeutic implications: 

Reversibility of Aβ oligomer neurotoxicity: Insights into the treatment of Alzheimer’s disease

 

 

Our work on the molecular organization of lipid rafts quoted in Wikipedia

(ref. 8 here)

 

J. Fantini H-index: 66

13075 citations

 

 

43000 visitors milestone reached!

Keywords

Publications

 

What Is life? Rethinking Biology in Light of Fundamental Parameters.

Fantini J, Matveeva M, Lefebvre M, Chahinian H.Life (Basel). 2024 Feb 20;14(3):280. doi: 10.3390/life14030280.

 

Emergence of a second SARS-CoV-2 variant with a tremendous genetic leap from its ancestors.Colson P, La Scola B, Beye M, Delerce J, Raoult D, Fantini J.J Med Virol. 2023 Oct;95(10):e29124.

Host Membranes as Drivers of Virus Evolution.Matveeva M, Lefebvre M, Chahinian H, Yahi N, Fantini J.Viruses. 2023 Aug 31;15(9):1854. doi: 10.3390/v15091854.

Lipid rafts and human diseases: why we need to target gangliosides.

Fantini J. FEBS Open Bio. 2023 Apr 13. doi: 10.1002/2211-5463.13612. Online ahead of print.PMID: 37052878 

 

Electrostatic Surface Potential as a Key Parameter in Virus Transmission and Evolution: How to Manage Future Virus Pandemics in the Post-COVID-19 Era.

Fantini J, Azzaz F, Chahinian H, Yahi N.Viruses. 2023 Jan 19;15(2):284. doi: 10.3390/v15020284.

 

Convergent Evolution Dynamics of SARS-CoV-2 and HIV Surface Envelope Glycoproteins Driven by Host Cell Surface Receptors and Lipid Rafts: Lessons for the Future.

Fantini J, Chahinian H, Yahi N.Int J Mol Sci. 2023 Jan 18;24(3):1923. doi: 10.3390/ijms24031

 

Structural basis of botulinum neurotoxin serotype A1 binding to human SV2A or SV2C receptors.

Azzaz F, Hilaire D, Fantini J.Chem Biol Interact. 2023 Mar 1;373:110384. doi: 10.1016/j.cbi.2023.110384.

 

AmyP53 Prevents the Formation of Neurotoxic β-Amyloid Oligomers through an Unprecedent Mechanism of Interaction with Gangliosides: Insights for Alzheimer's Disease Therapy.

Azzaz F, Chahinian H, Yahi N, Fantini J, Di Scala C.Int J Mol Sci. 2023 Jan 16;24(2):1760. doi: 10.3390/ijms24021760. 

 

 

 

 

The J. Fantini personal page has been created in September 2017

 

LinkedIn profile