DPhil in Developmental and Cell Biology
Postdoctoral Scientist in Molecular Neuroscience
Fascinated by Amyloidoisis, Protein folding, Aggregation pathways, Cell-to-cell spreading of amyloid protein aggregates.
After graduating from University of Rome "La Sapienza" (Italy) with degrees in Biological Science (BSc) and Molecular Biology (MSc), Livia obtained the PhD in Developmental and Cell Biology in 2005 in the University of Rome "La Sapienza" in collaboration with the École Normale Supérieure de Lyon (France).
From 2006 Livia has been investigating the neurodegenerative disorders, firstly, by studying the co-factorial role of Herpes simplex in the outcome of Alzheimer´s disease (AD). She produced data demonstrating that Herpes simplex infections trigger the amyloid-beta precursor protein (APP) processing, leading to the accumulation of multiple neurotoxic fragments and that infections significantly increases the extracellular content of Aβ. She also demonstrated that Herpes simplex infections induce the formation of a DNA-binding fragment that regulates the expression of specific genes involved in the outcome of AD.
From 2012-2017, Livia joined Linköping University (Sweden), where she started working on Aβ from a biophysical point of view. Livia studied the aggregation pathway of Aβ and the modulation of its toxic effect when aggregated together with luminescent conjugated oligothiophenes (LCOs). Livia demonstrated that the LCO pFTAA accelerates Aβ aggregation, thus counteracting Aβ cytotoxic effects as well as the LCO hFTAA can counteract the cytotoxic effect of Aβ with the Arctic mutation.
Livia´s research had also focused on cell-to-cell transfer of amyloid aggregates in both Alzheimer´s and Parkinson´s diseases via exosomes and/or diffusion and the possibility to impede either their uptake or the spreading among cells using specific antibodies as tools.
From 2018-2021, Livia studied at Linköping University where she obtained her second degree in Chemical Biology (MSc).
The Luminescent Conjugated Oligothiophene h-FTAA Attenuates the Toxicity of Different Aβ Species.
Sandin L. et al, (2021), Biochemistry
Inhibition of nSMase2 Reduces the Transfer of Oligomeric α-Synuclein Irrespective of Hypoxia
Sackmann V. et al, (2019), Frontiers in Molecular Neuroscience, 12
Lipid vesicles affect the aggregation of 4-hydroxy-2-nonenal-modified α-synuclein oligomers
Sardar Sinha M. et al, (2018), Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 1864, 3060 - 3068
Alzheimer’s disease pathology propagation by exosomes containing toxic amyloid-beta oligomers
Sardar Sinha M. et al, (2018), Acta Neuropathologica, 136, 41 - 56
The Luminescent Oligothiophene p-FTAA Converts Toxic Aβ1–42Species into Nontoxic Amyloid Fibers with Altered Properties
Civitelli L. et al, (2016), Journal of Biological Chemistry, 291, 9233 - 9243
Protective properties of lysozyme on β-amyloid pathology: implications for Alzheimer disease
Helmfors L. et al, (2015), Neurobiology of Disease, 83, 122 - 133