The understanding of protein aggregation is a central issue in different fields of protein science, from the heterologous protein production in biotechnology to amyloid aggregation in several neurodegenerative and systemic diseases. To this goal, it became more and more evident the crucial relevance of studying protein aggregation in the complex cellular environment, since it allows to take int...

Interfaces can strongly accelerate or inhibit protein aggregation, destabilizing proteins that are stable in solution or, conversely, stabilizing aggregation-prone. Although this behaviour is well-known, our understanding of the molecular mechanisms underlying surface-induced aggregation still largely incomplete. A major challenge represented by high number physico-chemical parameters involved,...

The presence of insoluble protein deposits in tissues and organs is a hallmark many human pathologies. In addition, the formation aggregates considered one main bottlenecks to producing protein-based therapeutics. Thus, there high interest rationalizing predicting aggregation. For almost two decades, our laboratory has been working provide solutions for these needs. We have traditionally combin...

Proteins aggregate in response to various stresses including changes in solvent conditions. Addition of alcohols has been recently shown to induce aggregation of disease-related as well as nondisease-related proteins. Here we probed the biophysical mechanisms underlying alcohol-induced protein aggregation, in particular the role of partial protein unfolding in aggregation. We have studied aggre...

Protein misfolding and aggregation have been considered important in understanding many neurodegenerative diseases and recombinant biopharmaceutical production. Therefore, various traditional and modern techniques have been utilized to monitor protein aggregation in vitro and in living cells. Fibril formation, morphology and secondary structure content of amyloidogenic proteins in vitro have be...

Lysine acetylation is becoming increasingly recognized as a general biological principle in cellular homeostasis, and is subject to abnormal control in different human pathologies. Here, we describe a global effect on amyloid-like protein aggregation in human cells that results from aberrant lysine acetylation. Bromodomain reader proteins are involved in the aggregation process and, using chemi...

ABSTRACTIntroduction: Cancer is caused by genetic abnormalities, such as mutation of ontogenesis or tumor suppressor genes which alter downstream signaling pathways and protein-protein interactions. Comparison of protein interactions in cancerous and normal cells can be of help in mechanisms of disease diagnoses and treatments. Methods: We constructed protein interaction networks of cancerous a...

Background: -synuclein is an aggregation-prone protein which reconfigures more slowly under aggregating conditions. Results: Curcumin binds to monomeric synuclein, prevents aggregation and increases the reconfiguration rate, particularly at high temperatures. Conclusion: Curcumin rescues the protein from aggregation by making the protein more diffusive. Significance: The search for aggregatio...

Hen egg white contains more than 40 kinds of proteins with concentrations reaching 100 mg/mL. Highly concentrated protein mixtures are common in the food industry, but the effects of a crowded environment containing salts on protein stability and aggregation have only been investigated using pure protein solutions. Here, we investigated the thermal aggregation of hen egg white protein (EWP) at ...