Certain peptide sequences in the protein, elastin, have a tendency to form long helical fibres when precipitated from aqueous suspension. The fibres are potentially useful as scaffolding for stem cell repair of human tissue. Prior studies of the structures and dimensions were made using chemically polymerised peptides that had a distribution of lengths. In this contribution to the topic we have used the molecule, (ValGlyGlyValGly)3 as a minimal component of elastin and show that this, too, forms helical assemblies. Using AFM of a single field of view we have obtained some key dimensions for the assemblies.
Characterisation of Helical Structure in AFM Micrographs of a Trimer of the Peptide Sequence (ValGlyGlyValGly)
SALVI, Anna Maria;BOCHICCHIO, Brigida;PEPE, Antonietta
2013-01-01
Abstract
Certain peptide sequences in the protein, elastin, have a tendency to form long helical fibres when precipitated from aqueous suspension. The fibres are potentially useful as scaffolding for stem cell repair of human tissue. Prior studies of the structures and dimensions were made using chemically polymerised peptides that had a distribution of lengths. In this contribution to the topic we have used the molecule, (ValGlyGlyValGly)3 as a minimal component of elastin and show that this, too, forms helical assemblies. Using AFM of a single field of view we have obtained some key dimensions for the assemblies.File in questo prodotto:
Non ci sono file associati a questo prodotto.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
