STUDY OF THE MOLECULAR BASIS OF BLOOD CLOT EXTENSIBILITY BY FTIR

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Fibers formed from fibrin (the primary protein in blood clots) are the most extensible biological polymers known, but the molecular basis for this extensibility has not been explored. We would like to use a custom-made clot stretcher to stretch oriented clots sandwiched between IR transparent windows to address this question by monitoring the amide I band using an FTIR spectrometer. We hope to observe secondary structural changes, specifically a potential alpha-helix to beta-sheet or random coil transition in blood clots for the first time under ambient conditions.