NR AXBL
AU Ghosh,S.; Verma,S.
TI Phased fiber growth in a peptide conjugate: aggregation and disaggregation studies.
QU The Journal of Physical Chemistry. B 2007 Apr 12; 111(14): 3750-7
PT journal article; research support, non-u.s. gov't
AB A glycine-rich, short pentapeptide conjugate 6, derived from the highly conserved copper-binding octarepeat region of the prion protein, exhibits a tendency to self-aggregate in a time-dependent fashion. Aging of 6 afforded an insight into the phased growth of spherical prefibrillar structures to fibers of long persistence length, as observed by a combination of microscopic techniques. Interestingly, growth of these fibers was inhibited 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 the formation of full length peptide fibers. It is also envisaged that constructs such as 6 may also serve as simple models to study chemical intervention of protein aggregation.
MH Conserved Sequence; Molecular Conformation; Multiprotein Complexes/*chemical synthesis/*chemistry; Oligopeptides/chemical synthesis/*chemistry; Prions/chemistry; Repetitive Sequences, Amino Acid; Stereoisomerism
AD Department of Chemistry, Indian Institute of Technology-Kanpur, Kanpur-208016 (UP), India.
SP englisch
PO USA