Research Team

Research Outlook


Our research at ULisboa aims to decipher molecular mechanisms underlying protein folding diseases.

We study protein aggregation mechanisms and its regulation by molecular chaperones in neurodegenerative diseases including  Alzheimer's Disease 

We also investigate loss of function due to protein misfolding in several mitochondrial metabolic and neurological diseases.


We combine molecular, cellular and biochemical experimental approaches to investigate protein structure and self-assembly in vitro and in cells.

Implemented techniques comprise:
● Purification of disease causing proteins (Aβ, Tau, Syn)
● Mechanistic analysis of amyloid aggregation kinetics;
● Structural biophysics analysis (CD, ATR-FTIR fluorescence)
● Enzymatic assays (ETC, β-oxidation)
● cell toxicity and RT-QuIC assays.


The laboratory is a vibrant workplace composed by passionate and curious team members from different backgrounds, nationalities and training levels.

Team effort is driven by high-quality, thorough research in protein biochemistry and biophysics.

We regularly welcome visiting professors in sabbatical periods and international students in short term research internships.


Through collaboration we summon knowledge, methodological resources and training opportunities for team members that allow tackling our research questions in a multidisciplinary perspective, from molecules, to cells to organisms.

Our collaborative network includes +10 research institutions worldwide and includes physicists, computational biologists, mathematicians, cell biologists and clinicians.

Protein aggregation and amyloids in neurodegeneration

Mechanisms of
amyloid formation

Understanding the mechanistic aspects of protein self-assembly and amyloid formation  is critical to establish cellular and molecular modulators of protein aggregation in the diseased brain.

Through kinetics and mechanistic analysis, we are investigating amyloid formation by Aβ, Tau and Syn.

We seek to establish how cellular conditions, small molecules and antibodies influence protein aggregation, to assist in defining better therapies.

 Cristóvão et al (2018) Sci. Adv.
 Moreira et al (2019) IJMS

S100 proteins in Alzheimer’s Disease 

S100 proteins are recognized biomarkers for brain distress in neurodegenerative conditions including Alzheimer’s.

We seek to uncover novel molecular mechanisms implicating S100 proteins, that link aggregation and neuroinflammation cascades.

For instance, we are combining in vitro assays and studies in animal models to analyse expression levels of S100 proteins in correlation with their spatial distribution within neuronal protein inclusions.

Inhibitors of
amyloid formation

We recently uncovered novel neuro-protective functions which imply S100 alarmins in vital house-keeping processes that harness AD.

Specifically, we found that under physiological conditions mimicking early disease states, S100B acts as a new type of molecular chaperone delaying aggregation.

This is achieved through binding of monomeric Aβ to S100B.

Ongoing research is further dissecting the function of these chaperones, combining spectroscopic, molecular, and kinetic approaches

Brain metal ions and protein aggregation 

In neurodegeneration, imbalance in metal ion homeostasis results in altered homeostasis with deleterious consequences.

On the one hand, we are investigating how metal-protein interactions influence protein aggregation and the oligomers landscape.

On the other hand, we focus on metal binding proteins that can act as scavengers regulating amyloid aggregation and toxicity.

 Moreira et al (2019) IJMS
 Hagmeyer (2018) Front Mol Neurosci
 Leal et al (2012) Coord. Chem. Rev.

Protein misfolding in mitochondrial diseases