@article{2710169,
    title = "An N-terminal pro-atrial natriuretic peptide (NT-proANP) 'aggregation-prone' segment involved in isolated atrial amyloidosis.",
    author = "Nikolaos Louros and Vassiliki Iconomidou and Paraskevi Tsiolaki and Evangelia Chrysina and Georgios Baltatzis and Eustratios Patsouris and Stavros Hamodrakas",
    journal = "FEBS Letters",
    year = "2014",
    volume = "588",
    number = "1",
    pages = "52-57",
    publisher = "Wiley",
    issn = "0014-5793",
    keywords = "Natriuretic peptide, N-terminal pro-atrial natriuretic peptide (NT-proANP), Amyloid fibril, Isolated atrial amyloidosis (IAA), Cardiac amyloidose",
    abstract = "Isolated 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
(
114KLRALLT120) 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)"
}