TY - JOUR
T1 - Probing the interactions between amyloidogenic proteins and bio-membranes
AU - Ma, Liang
AU - Li, Xi
AU - Petersen, Robert B.
AU - Peng, Anlin
AU - Huang, Kun
N1 - Funding Information:
We sincerely appreciate the investigators and authors who have contributed to this field and apologize that we could not discuss and cite all of them in this review due to space limitations. This work was supported by the National Key R&D Program of China (2022YFA0806100), the Natural Science Foundation of China (NSFC No. 81901302, 82273838, 31971066 and 31671195), the Wuhan Municipal Health Research Foundation (WZ20Q02), Wuhan Municipal Health Youth Talent Training Program, the Key project of the Natural Science Foundation of Hubei Province (2021CFA004), Science and Technology Program of Hubei Province (2022DFE025) and Integrated Innovative Team for Major Human Diseases Program of Tongji Medical College, HUST.
Funding Information:
We sincerely appreciate the investigators and authors who have contributed to this field and apologize that we could not discuss and cite all of them in this review due to space limitations. This work was supported by the National Key R&D Program of China ( 2022YFA0806100 ), the Natural Science Foundation of China (NSFC No. 81901302 , 82273838 , 31971066 and 31671195 ), the Wuhan Municipal Health Research Foundation ( WZ20Q02 ), Wuhan Municipal Health Youth Talent Training Program , the Key project of the Natural Science Foundation of Hubei Province ( 2021CFA004 ), Science and Technology Program of Hubei Province ( 2022DFE025 ) and Integrated Innovative Team for Major Human Diseases Program of Tongji Medical College , HUST .
Publisher Copyright:
© 2023
PY - 2023/5
Y1 - 2023/5
N2 - 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.
AB - 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.
KW - Amyloidogenic proteins
KW - Detecting
KW - Interaction
KW - Membrane
KW - Therapeutic strategies
UR - http://www.scopus.com/inward/record.url?scp=85149462142&partnerID=8YFLogxK
U2 - 10.1016/j.bpc.2023.106984
DO - 10.1016/j.bpc.2023.106984
M3 - Review article
C2 - 36889133
AN - SCOPUS:85149462142
SN - 0301-4622
VL - 296
JO - Biophysical Chemistry
JF - Biophysical Chemistry
M1 - 106984
ER -
