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 ((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).
Keywords: AF; ANP; ATR FT-IR spectroscopy; Amyloid fibril; BNP; CHF; Cardiac amyloidose; IAA; Isolated atrial amyloidosis (IAA); N-terminal pro-atrial natriuretic peptide; N-terminal pro-atrial natriuretic peptide (NT-proANP); NT-proANP; Natriuretic peptide; SSA; TTR; atrial fibrosis; atrial natriuretic peptide; attenuated total reflectance Fourier-transform spectroscopy; brain natriuretic peptide; cGMP; congestive heart failure; cyclic guanosine monophosphate; isolated atrial amyloidosis; senile systemic amyloidosis; transthyretin.
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