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FEBS Lett. 2015 Jan 2;589(1):159-64. doi: 10.1016/j.febslet.2014.11.041. Epub 2014 Dec 3.

The pentapeptide LQVVR plays a pivotal role in human cystatin C fibrillization.

Author information

1
Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens 157 01, Greece.
2
Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens 157 01, Greece. Electronic address: veconom@biol.uoa.gr.

Abstract

Human cystatin C (HCC) is a low molecular weight member of the cystatin family (type2). HCC consists of 120 amino acids. Normally it is an inhibitor of cysteine proteases, but in pathological conditions it forms amyloid fibrils in brain arteries of young adults. An 'aggregation-prone' pentapeptide ((47)LQVVR(51)) was located within the HCC sequence using AmylPred, an 'aggregation-prone' peptide prediction algorithm developed in our lab. This peptide was synthesized and self-assembled into amyloid-like fibrils in vitro, as electron microscopy, X-ray fiber diffraction, Attenuated Total Reflectance Fourier-Transform Spectroscopy and Congo red staining studies reveal. Thus, the (47)LQVVR(51) peptide seems to have an important role in HCC fibrillization.

KEYWORDS:

3D-domain swapping; Alzheimer’s disease; Amyloid fibrils; Hereditary Cystatin C Amyloid Angiopathy; Human cystatin C; ‘Aggregation-prone’ pentapeptide LQVVR

PMID:
25479090
DOI:
10.1016/j.febslet.2014.11.041
[Indexed for MEDLINE]
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