The α-helix to β-sheet transition in stretched and compressed hydrated fibrin clots.

ABSTRACT: Fibrin is a protein polymer that forms the viscoelastic scaffold of blood clots and thrombi. Despite the critical importance of fibrin deformability for outcomes of bleeding and thrombosis, the structural origins of the clot's elasticity and plasticity remain largely unknown. However, there is substantial evidence that unfolding of fibrin is an important part of the mechanism. We used Fourier transform infrared spectroscopy to reveal force-induced changes in the secondary structure of hydrated fibrin clots made of human blood plasma in vitro. When extended or compressed, fibrin showed a shift of absorbance intensity mainly in the amide I band (1600-1700 cm(-1)) as well as in the amide II and III bands, indicating an increase of the β-sheets and a corresponding reduction of the α-helices. T

SUBMITTER: Litvinov RI 

PROVIDER: S-EPMC3433599 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature