title: Direct observation and pH control of reversed supramolecular chirality in insulin fibrils by vibrational circular dichroism.
abstract: The controlled reversal of supramolecular helical chirality in protein fibrils is reported for the first time. Normal or reversed insulin fibrils were grown by precise adjustment of pH. AFM images show two polymorphs corresponding to opposite senses of helical twist of the supramolecular structure with the same cross-β-sheet core.
authors.affiliation: Department of Chemistry, University at Albany, SUNY, 1400 Washington Ave., Albany, NY 12222, USA.
authors.forename: Dmitry
authors.initials: D
authors.lastname: Kurouski
authors.forename: Rosina A
authors.initials: RA
authors.lastname: Lombardi
authors.forename: Rina K
authors.initials: RK
authors.lastname: Dukor
authors.forename: Igor K
authors.initials: IK
authors.lastname: Lednev
authors.forename: Laurence A
authors.initials: LA
authors.lastname: Nafie
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D007328:Insulin / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D017433:Protein Structure, Secondary
chemical_list: D000682:Amyloid; D007328:Insulin