Structural Mechanisms of Forced Unfolding of Double-Stranded Fibrin Oligomers.

ABSTRACT: Fibrin forms a polymeric scaffold of blood clots, which are subjected to deformation in their dynamic environment. The extensible fibrin network allows fibers to stretch without breaking, but the mechanisms of their forced elongation are not understood. We combined atomic force microscopy, computer simulations, and Machine Learning to explore the nanomechanics of double-stranded cross-linked fibrin oligomers (FO). From the experimental force-extension profiles, the median 63 pN unfolding force and median 8.1 nm peak-to-peak distance with corresponding 56 pN and 11.4 nm interquartile ranges indicate substantial scatter due to ∼3-5 nm extension fluctuation of the triple α-helical coiled-coils. From simulations, unraveling of FO is determined by coupled dissociation of the D:D interface, γ-no

SUBMITTER: Maksudov F 

PROVIDER: S-EPMC12035854 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature