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* Department of Physics, Wake Forest University, Winston-Salem, North Carolina;
Department of Pathology and Lab Medicine, University of North Carolina, Chapel Hill, North Carolina;
Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem, North Carolina; and ¶ Departments of Chemistry,
Computer Science, and || Physics, University of North Carolina, Chapel Hill, North Carolina
Correspondence: Address reprint requests to Asst. Prof. Martin Guthold, Dept. of Physics, Wake Forest University, Reynolda Station 7507, Winston-Salem, NC 27109. Tel.: 336-758-4977; E-mail: gutholdm{at}wfu.edu.
We report protocols and techniques to image and mechanically manipulate individual fibrin fibers, which are key structural components of blood clots. Using atomic force microscopy-based lateral force manipulations we determined the rupture force, FR, of fibrin fibers as a function of their diameter, D, in ambient conditions. As expected, the rupture force increases with increasing diameter; however, somewhat unexpectedly, it increases as FR
D1.30±0.06. Moreover, using a combined atomic force microscopy-fluorescence microscopy instrument, we determined the light intensity, I, of single fibers, that were formed with fluorescently labeled fibrinogen, as a function of their diameter, D. Similar to the force data, we found that the light intensity, and thus the number of molecules per cross section, increases as I
D1.25±0.11. Based on these findings we propose that fibrin fibers are fractals for which the number of molecules per cross section increases as about D1.3. This implies that the molecule density varies as
(D)
D0.7, i.e., thinner fibers are denser than thicker fibers. Such a model would be consistent with the observation that fibrin fibers consist of 7080% water and only 2030% protein, which also suggests that fibrin fibers are very porous.
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