Synthetic VGGVG, a "monomeric" unit of the glycine-rich regions of elastin, has been investigated for its molecular and supramolecular properties. In aqueous solution the pentapeptide showed conformational features strongly concentration-dependent. CD and NMR studies suggested a partial unfolding on increasing the concentration. Electron microscopy, on the other hand, evidenced extensive aggregation of the pentapeptide yielding elastin-like supramolecular structures constituted either by twisted ropes or by banded fibrils.
An aggregating elastin-like pentapeptide
DE STRADIS A;
1993
Abstract
Synthetic VGGVG, a "monomeric" unit of the glycine-rich regions of elastin, has been investigated for its molecular and supramolecular properties. In aqueous solution the pentapeptide showed conformational features strongly concentration-dependent. CD and NMR studies suggested a partial unfolding on increasing the concentration. Electron microscopy, on the other hand, evidenced extensive aggregation of the pentapeptide yielding elastin-like supramolecular structures constituted either by twisted ropes or by banded fibrils.File in questo prodotto:
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