Protein self-assembly in health and disease
Life arises from the organization of disordered matter into ordered, functional structures. In cells, this order emerges through dynamic molecular processes, including the self-assembly of proteins into complex molecular machinery that enables adaptation and survival. Our research group examines how protein conformational changes and self-assembly — including protein phase separation, aggregation, and amyloid formation — regulate cellular behavior in health and disease. Drawing on concepts and methodologies from the life and physical sciences, we uncover how protein self-assembly is regulated, how it shapes cellular function, and how it can be harnessed for therapeutic intervention and biomolecular engineering. We study these processes in the context of immune responses and aging, positioning our work at the interface of fundamental and biomedical research.
Research Areas - Protein Self-Assembly in...
Immune Signaling
We study how protein phase separation and aggregation of immune signaling proteins regulate cellular communication, decision-making, and stress responses. This work reveals how changes in protein conformation reshape immune signaling in health and during aging.
Immune Defense
We investigate how antimicrobial peptides and innate immune proteins self-assemble into condensates and amyloid-like structures to enable robust and adaptable host defense. By linking molecular assembly to cellular function, we uncover new principles of antimicrobial immunity.
Cellular Stress & Aging
We explore how cellular stress conditions influence protein self-assembly, reversibility, and material properties. This research examines how stress adaptation and aging shape protein condensate behavior and cellular resilience and how failures in this processes contribute to diseases.
Our Techniques
Cellular
Functional Assays
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Fluorescence Imaging
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Protein Biochemistry
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Microfluidic
Assays
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“Nothing in life is to be feared. It is only to be understood”
Marie Skłodowska-Curie
