Ultrastructural organization of ex vivo amyloid fibrils formed by the apolipoprotein A-I Leu174Ser variant: An atomic force microscopy study

Annalisa Relini, Ranieri Rolandi, Martino Bolognesi, Manuela Aboudan, Giampaolo Merlini, Vittorio Bellotti, Alessandra Gliozzi

Research output: Contribution to journalArticlepeer-review

Abstract

Atomic force microscopy was employed to study ex vivo amyloid material isolated from the transplanted hearts of two patients affected by systemic amyloidosis caused by the Leu174Ser apolipoprotein A-I variant. The purified material consists of fibrils and globular aggregates. For both patients the same morphological patterns are observed; in addition, fibril diameters obtained for the two patients turn out to be compatible, both in air (2.00±0.02 and 2.04±0.04 nm) and under liquid (10.7±0.4 and 11.3±0.5 nm). Fibrils display heterogeneous morphologies, occasionally showing a left-handed twist. Inspection of fibril ends, the study of fibril contour shape and the analysis of partially unfolded fibrils yield independent evidences suggesting that most twisted fibrils are composed of three protofilaments. The size of globular aggregates is the same for both patients (4.4±0.4 and 5.1±0.5 nm, measured under liquid) and is compatible with the protofilament expected diameter, suggesting that globules may represent protofilament precursors.

Original languageEnglish
Pages (from-to)33-41
Number of pages9
JournalBiochimica et Biophysica Acta - Molecular Basis of Disease
Volume1690
Issue number1
DOIs
Publication statusPublished - Sep 6 2004

Keywords

  • Amyloid
  • Apolipoprotein A-I
  • Atomic force microscopy

ASJC Scopus subject areas

  • Molecular Biology
  • Molecular Medicine
  • Biophysics

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