Toward determining amyloid fibril structures using experimental constraints from Raman spectroscopy
Conference Year
2024
Abstract
Amyloid fibrils are β-sheet rich protein aggregates that are implicated in diseases such as Alzheimer’s. Using Raman Spectroscopy, we demonstrated the distributions of peptide backbone amide C=O bond orientation and Ramachandran ψ dihedral angles can effectively guide molecular dynamics (MD) simulations to build structural models of amyloid fibrils. Our model systems, amylin20−29 and amyloid-β (Aβ)25−35, are oriented inextended β-sheet strands that are either parallel (amylin20−29 and Aβ25−35) or antiparallel (amylin20−29) β-sheet structures. Overall, our work lays the foundation for utilizing Raman spectroscopy as structural constraints in MD simulations to determine the three-dimensional molecular structural models of amyloid fibrils.
Primary Faculty Mentor Name
David Punihaole
Status
Graduate
Student College
College of Arts and Sciences
Program/Major
Chemistry
Primary Research Category
Physical Science
Toward determining amyloid fibril structures using experimental constraints from Raman spectroscopy
Amyloid fibrils are β-sheet rich protein aggregates that are implicated in diseases such as Alzheimer’s. Using Raman Spectroscopy, we demonstrated the distributions of peptide backbone amide C=O bond orientation and Ramachandran ψ dihedral angles can effectively guide molecular dynamics (MD) simulations to build structural models of amyloid fibrils. Our model systems, amylin20−29 and amyloid-β (Aβ)25−35, are oriented inextended β-sheet strands that are either parallel (amylin20−29 and Aβ25−35) or antiparallel (amylin20−29) β-sheet structures. Overall, our work lays the foundation for utilizing Raman spectroscopy as structural constraints in MD simulations to determine the three-dimensional molecular structural models of amyloid fibrils.