Stepwise dynamics of epitaxially growing single amyloid fibrils

Miklós S.Z. Kellermayer, Árpád Karsai, Margit Benke, Katalin Soós, Botond Penke

Research output: Article

78 Citations (Scopus)


The assembly mechanisms of amyloid fibrils, tissue deposits in a variety of degenerative diseases, is poorly understood. With a simply modified application of the atomic force microscope, we monitored the growth, on mica surface, of individual fibrils of the amyloid β25-35 peptide with near-subunit spatial and subsecond temporal resolution. Fibril assembly was polarized and discontinuous. Bursts of rapid (up to 300-nm-1) growth phases that extended the fibril by ≈7 nm or its integer multiples were interrupted with pauses. Stepwise dynamics were also observed for amyloid β1-42 fibrils growing on graphite, suggesting that the discontinuous assembly mechanisms may be a general feature of epitaxial amyloid growth. Amyloid assembly may thus involve fluctuation between a fast-growing and a blocked state in which the fibril is kinetically trapped because of intrinsic structural features. The used scanning-force kymography method may be adapted to analyze the assembly dynamics of a wide range of linear biopolymers.

Original languageEnglish
Pages (from-to)141-144
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number1
Publication statusPublished - jan. 8 2008

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Stepwise dynamics of epitaxially growing single amyloid fibrils'. Together they form a unique fingerprint.

  • Cite this