Supramolecular chirality in peptide microcrystals. Academic Article

abstract

• The vibrational circular dichroism (VCD) spectra of microcrystals of fibril-forming peptides have been measured for the first time. VCD spectra were measured and compared for microcrystals and fibrils formed from the same peptide, human islet amyloid polypeptide (IAPP, amylin). Structural information related to the supramolecular chirality of both the microcrystals and the fibrils, as well as the VCD enhancement mechanisms in fibrils and microcrystals, is obtained from these spectral comparisons. It is concluded that strongly enhanced VCD does not require braiding of two or more filaments that is permitted in fibrils but not microcrystals.

authors

• Kurouski, Dzmitry

published proceedings

• Chem Commun (Camb)

author list (cited authors)

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

citation count

• 27

complete list of authors

• Kurouski, Dmitry||Handen, Joseph D||Dukor, Rina K||Nafie, Laurence A||Lednev, Igor K

publication date

• January 2015

publisher

• Royal Society of Chemistry (RSC)  Publisher

published in

• Chemical Communications  Journal

keywords

• Amino Acid Sequence
• Circular Dichroism
• Crystallization
• Humans
• Islet Amyloid Polypeptide
• Protein Structure, Secondary
• Stereoisomerism

PubMed Central ID

• 25351531

Digital Object Identifier (DOI)

• 10.1039/c4cc05002a

start page

• 89

end page

• 92

volume

• 51

issue

• 1

URL

• http://dx.doi.org/10.1039/c4cc05002a