| Abstract
| - A glycine-rich, short pentapeptide conjugate 6, derived from the highly conserved copper-binding octarepeatregion of the prion protein, exhibits a tendency to self-aggregate in a time-dependent fashion. Aging of 6afforded an insight into the phased growth of spherical prefibrillar structures to fibers of long persistencelength, as observed by a combination of microscopic techniques. Interestingly, growth of these fibers wasinhibited by colchicine, a known inhibitor of microtubule polymerization in a concentration dependent fashion.This study offers an intriguing insight into the occurrence of prefibrillar intermediates on the path to theformation of full length peptide fibers. It is also envisaged that constructs such as 6 may also serve as simplemodels to study chemical intervention of protein aggregation.
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