LL-37 and CsgC exemplify the crosstalk between anti-amyloid,antimicrobial,and anti-biofilm protein activities
Jaime Santos
Salvador Ventura
Irantzu Pallarès
Institut de Biotecnologia i Biomedicina,Departament de Bioquímica i Biologia Molecular,Universitat Autònoma de Barcelona,Bellaterra,Barcelona,Spain
摘要：Protein misfolding and aggregation into amyloid fibrils is the main pathological hallmark of neurodegenerative diseases,including Alzheimer's,Parkinson's,Huntington's,and prion diseases(Chiti and Dobson,2017).These insoluble fibrillar deposits possess a common structure characterized by a cross-β-sheet conformation in which β-strands run transversely to the fiber axis and form an intermolecular network of hydrogen bonds.However,amyloid formation is not only found in disease;the unique properties of this protein fold are also exploited by nature to perform a growing list of relevant and highly conserved cellular functions(Otzen and Riek,2019).Pathogenic and functional amyloid formation needs to be regulated to sustain organism fitness,and a wide range of strategies have evolved to prevent uncontrolled aggregation.Importantly,we are not only exposed to our endogen amyloidogenic proteins,but we also face the threat of food and bacterial amyloids.
机标关键词：crosstalkproteinbetweencsgcactivitiesanti-amyloidanti-biofilmantimicrobial
论文发表日期：2023-05-28
在线出版日期：2025-08-15（本平台首次上网日期，不代表文献的发表时间）
页数：2( 1027-1028 )