Probing the interactions between amyloidogenic proteins and bio-membranes

Liang Ma, Xi Li, Robert B. Petersen, Anlin Peng, Kun Huang

Research output: Contribution to journalReview articlepeer-review


Protein misfolding diseases (PMDs) in humans are characterized by the deposition of protein aggregates in tissues, including Alzheimer's disease, Parkinson's disease, type 2 diabetes, and amyotrophic lateral sclerosis. Misfolding and aggregation of amyloidogenic proteins play a central role in the onset and progression of PMDs, and these processes are regulated by multiple factors, especially the interaction between proteins and bio-membranes. Bio-membranes induce conformational changes in amyloidogenic proteins and affect their aggregation; on the other hand, the aggregates of amyloidogenic proteins may cause membrane damage or dysfunction leading to cytotoxicity. In this review, we summarize the factors that affect the binding of amyloidogenic proteins and membranes, the effects of bio-membranes on the aggregation of amyloidogenic proteins, mechanisms of membrane disruption by amyloidogenic aggregates, technical approaches for detecting these interactions, and finally therapeutic strategies targeting membrane damage caused by amyloidogenic proteins.

Original languageEnglish
Article number106984
JournalBiophysical Chemistry
StatePublished - May 2023


  • Amyloidogenic proteins
  • Detecting
  • Interaction
  • Membrane
  • Therapeutic strategies


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