An aggregating elastin-like pentapeptide.

M A Morelli; M DeBiasi; A DeStradis; A M Tamburro

doi:10.1080/07391102.1993.10508716

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An aggregating elastin-like pentapeptide.

M A Morelli·M DeBiasi·A DeStradis·A M Tamburro

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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.

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Amino Acid Sequence Circular Dichroism Elastin Magnetic Resonance Spectroscopy Microscopy, Electron Molecular Sequence Data Oligopeptides Protein Conformation Comparative Study Journal Article Research Support, Non-U.S. Gov't

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M A Morelli, M DeBiasi, A DeStradis, A M Tamburro. 1993. An aggregating elastin-like pentapeptide.. https://doi.org/10.1080/07391102.1993.10508716

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