| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1930902 | Biochemical and Biophysical Research Communications | 2011 | 5 Pages |
The misfolding and aggregation of proteins is associated with many different diseases including the trinucleotide repeat disorders and Prion diseases. We have studied three residue peptides comprising alanine and glutamine in order to understand the short range interactions affecting the formation of β-rich aggregates. Using infrared spectroscopy, we have found that trialanine and triglutamine form significant amounts of β-sheet, but that tripeptides containing alanine and glutamine are only able to form β-sheet if the glutamine side-chains extend outward on both faces of the sheet. From our data, we conclude that different stabilizing interactions are responsible for β-sheet formation in trialanine and triglutamine.
Research highlights► We use IR spectroscopy to study β-sheet formation in alanine and glutamine peptides. ► β-Sheets are stabilized by packing of methyl side-chains of alanine. ► β-Sheets are stabilized by side-chain to side-chain hydrogen bonding of glutamine. ► β-Sheet orientation and stability depends on amino acid sequence.
