Protein Structure and Aggregation.

Proteins are dynamic biomolecules whose structures and interactions with their surrounding environment determine their biological function. Changes in protein conformation induced by drugs, surfaces, membranes, or nanomaterials can alter their activity, promote aggregation, or trigger the formation of amyloid structures associated with numerous diseases. Understanding these processes is essential for the rational design of biomaterials, nanomedicines, and therapeutic strategies.

At Nano4Med, we investigate how proteins and peptides interact with nanoparticles, biomimetic membranes, solid surfaces, and bioactive compounds. Using complementary biophysical and spectroscopic techniques, we characterize protein adsorption, conformational changes, and aggregation mechanisms under physiologically relevant conditions. These studies provide molecular-level insights into the factors governing protein stability, folding, and self-assembly.

Our research also focuses on amyloidogenic proteins and peptides, aiming to understand the molecular mechanisms underlying protein aggregation and to identify compounds that modulate or inhibit amyloid formation. By integrating biomimetic membrane models, we evaluate protein behavior in environments that more closely resemble biological systems, contributing to the development of innovative therapeutic approaches for protein misfolding diseases.

Our Research Includes

• Protein–nanoparticle interactions

• Protein–membrane interactions

• Protein adsorption onto solid surfaces

• Protein conformational analysis

• Protein aggregation and amyloid formation

Our Studies Contribute to

• Understanding protein structure and stability

• Elucidating protein aggregation mechanisms

• Developing anti-amyloid therapeutic strategies

• Designing safer nanomaterials and biomaterials

• Advancing nanomedicine and neurodegenerative disease research

​

​

​​