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The pentapeptide LQVVR plays a pivotal role in human cystatin C fibrillization
Author(s) -
Tsiolaki Paraskevi L.,
Hamodrakas Stavros J.,
Iconomidou Vassiliki A.
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.11.041
Subject(s) - pentapeptide repeat , congo red , peptide , fibril , cystatin , amyloid (mycology) , chemistry , biochemistry , cystatin c , in vitro , biophysics , biology , inorganic chemistry , organic chemistry , adsorption , renal function
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.