• FEBS letters · Jan 2014

    An N-terminal pro-atrial natriuretic peptide (NT-proANP) 'aggregation-prone' segment involved in isolated atrial amyloidosis.

    • Nikolaos N Louros, Vassiliki A Iconomidou, Paraskevi L Tsiolaki, Evangelia D Chrysina, Georgios E Baltatzis, Efstratios S Patsouris, and Stavros J Hamodrakas.
    • Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens 157 01, Greece.
    • FEBS Lett. 2014 Jan 3; 588 (1): 52-7.

    AbstractIsolated atrial amyloidosis (IAA) is a common localized form of amyloid deposition within the atria of the aging heart. The main constituents of amyloid fibrils are atrial natriuretic peptide (ANP) and the N-terminal part of its precursor form (NT-proANP). An 'aggregation-prone' heptapeptide ((114)KLRALLT(120)) was located within the NT-proANP sequence. This peptide self-assembles into amyloid-like fibrils in vitro, as electron microscopy, X-ray fiber diffraction, ATR FT-IR spectroscopy and Congo red staining studies reveal. Consequently, remedies/drugs designed to inhibit the aggregation tendency of this 'aggregation-prone' segment of NT-proANP may assist in prevention/treatment of IAA, congestive heart failure (CHF) or atrial fibrillation (AF). Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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