TY - JOUR
TI - An N-terminal pro-atrial natriuretic peptide (NT-proANP) 'aggregation-prone' segment involved in isolated atrial amyloidosis.
AU - Nikolaos Louros
AU - Vassiliki Iconomidou
AU - Paraskevi Tsiolaki
AU - Evangelia Chrysina
AU - Georgios Baltatzis
AU - Eustratios Patsouris
AU - Stavros Hamodrakas
JO - FEBS Letters
PY - 2014
VL - 588
TODO - 1
SP - 52-57
PB - Wiley
SN - 0014-5793
TODO - null
TODO - Natriuretic peptide, N-terminal pro-atrial natriuretic peptide (NT-proANP), Amyloid fibril, Isolated atrial amyloidosis (IAA), Cardiac amyloidose
TODO - 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)
ER -