Direct observation and pH control of reversed supramolecular chirality in insulin fibrils by vibrational circular dichroism. Academic Article

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--sheet core.

authors

• Kurouski, Dzmitry

published proceedings

• Chem Commun (Camb)

author list (cited authors)

• Kurouski, D., Lombardi, R. A., Dukor, R. K., Lednev, I. K., & Nafie, L. A.

citation count

• 106

complete list of authors

• Kurouski, Dmitry||Lombardi, Rosina A||Dukor, Rina K||Lednev, Igor K||Nafie, Laurence A

publication date

• October 2010

publisher

• Royal Society of Chemistry (RSC)  Publisher

published in

• Chemical Communications  Journal

keywords

• Amyloid
• Circular Dichroism
• Hydrogen-Ion Concentration
• Insulin
• Microscopy, Atomic Force
• Protein Structure, Secondary

PubMed Central ID

• 20820535

Digital Object Identifier (DOI)

• 10.1039/c0cc02423f

start page

• 7154

end page

• 7156

volume

• 46

issue

• 38

URL

• http://dx.doi.org/10.1039/c0cc02423f