Abstract
The N-capping region of an alpha-helix is a short N-terminal amino acid stretch that contributes to nucleate and stabilize the helical structure. In the VEGF mimetic helical peptide QK, the N-capping region was previously demonstrated to be a key factor of QK helical folding. In this paper, we explored the effect of the chiral inversion of the N-capping sequence on QK folding, performing conformational analysis in solution by circular dichroism and NMR spectroscopy. The effect of such a modification on QK stability in serum and the proliferative effect were also evaluated.
Lingua originale | Inglese |
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Rivista | Molecules |
Volume | 27 |
Numero di pubblicazione | 20 |
DOI | |
Stato di pubblicazione | Pubblicato - 2022 |
Keywords
- D-amino acid
- N-capping
- NMR
- peptide conformation
- peptide folding
- α-helix