Protofibrils within fibrin fibres are packed together in a regular array
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Updated: Sep 26, 2026

Amyloid and the Cross-Beta Architecture
Published on: February 13, 2026
Giulio Caracciolo1, Marco De Spirito, Agostina Congiu Castellano
1Dept of Biochemical Sciences, University of Rome La Sapienza, Piazzale Aldo Moro 5, I-00185 Rome, Italy.
Abstract:
The inner structure of fibrin fibres grown from fibrinogen solution activated by human alpha-thrombin was investigated by means of an Energy Dispersive X-ray Diffraction technique. The experiments show evidence for the well-characterized 22.5 nm repeat distance, which indicates the high order of protofibril arrangement in the longitudinal direction of fibres. The diffraction pattern also manifested a further pronounced peak at 18.1 nm (and its second order reflection at 18.1/ radical 2) demonstrating the existence in fibrin of a high degree of lateral order. The reported results directly confirm, on unperturbed wet samples, that protofibrils closely associate giving rise to a crystalline axial and equatorial packing according to the conclusions of the multibundle model.
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