This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.Regeneration and protection of the cardiovascular system is essential for vertebrates. Blood clots (solid yet elastic clumps of blood cells mixed with fibrin proteins) form part of the emergency response to an injured blood vessel; they surround the damaged tissue stopping bleeding and blocking invasion by foreign pathogens. On the other hand, blood clots can restrict essential and normal blood flow if they form at the wrong place, or break free from a larger vessel only to later block a smaller one (thrombosis) [1]. Therefore, blood clots must be stiff enough to seal wounded vessels, yet flexible to prevent breakage and subsequent blockage of small vessels [2].Blood clots are built from red blood cells and a protein called fibrinogen. In its active form, fibrinogen is converted by thrombin into fibrin, which polymerizes into a branched network to form a hemostatic plug in combination with platelets and blood clotting factors [3,4]. The mechanical properties of blood clots are highly dependent on both the network architecture of fibrin and the mechanical properties of fibrin's individual components [4].Interactions between paired chains of fibrin and fibrinogen have been described by several recent studies that stretched these molecules using both optical tweezers [5, 6, 7] and atomic force microscopy (AFM)[8]. However, the elastic properties of single fibrinogen molecules and their coiled-coil helices, the predominant structures along the length of the molecule, remain unclear.
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