Structure and Formation Mechanism of Amyloid Fibrils
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".
Deadline for manuscript submissions: closed (30 April 2024) | Viewed by 2361
Special Issue Editors
Interests: amyloid; biopolymers; infrared laser; terahertz radiation
Special Issues, Collections and Topics in MDPI journals
Interests: amyloid; molecular dynamics of protein; RNA and lipid membrane
Special Issue Information
Dear Colleagues,
Amyloid fibrils are known to cause serious diseases such as neurodegenerative diseases and amyloidosis. Recently, it has been reported that lower-molecular-sized oligomers are found to be more toxic in cells than mature fibrils. The technology for the degradation of those amyloid assemblies has the potential for leading to amyloidosis therapy. However, the formation mechanism of amyloid fibrils is not completely understood, and it is usually difficult to degrade the rigid fibrous conformation under mild conditions unless using denaturants. This special issue welcomes structural studies focusing on the fibrils, proto-fibrils, and oligomers of various types of amyloid peptides and proteins. Especially uses of not only experimental techniques but also computer simulation methods for approaching the formation mechanisms of amyloid assemblies are acceptable. In addition, application studies of physical engineering techniques such as lasers and high-power radiations to develop novel therapeutic ways for amyloidosis should also be welcome.
Dr. Takayasu Kawasaki
Dr. Phuong H. Nguyen
Guest Editors
Manuscript Submission Information
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Keywords
- amyloid fibril
- oligomer
- proto-fibril
- molecular simulation
- laser
- radiation
