AI Article Synopsis
- The first measurement of vibrational circular dichroism (VCD) spectra for microcrystals of fibril-forming peptides, specifically human islet amyloid polypeptide (IAPP), was conducted.
- The study compared the VCD spectra of microcrystals and fibrils from the same peptide to gather insights into their structural characteristics and supramolecular chirality.
- It was found that enhanced VCD in these structures does not depend on the twisting of multiple filaments, which is a characteristic of fibrils but not microcrystals.
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.
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| http://dx.doi.org/10.1039/c4cc05002a | DOI Listing |
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