Sickle hemoglobin (HbS) is a genetic alteration of normal hemoglobin A (HbA). In HbS, a surface amino acid (b6) is transformed from charged (Glu) to hydrophobic (Val). This leads to the formation of multi-stranded polymers, which in turn are found in interconnected arrays called domains. The polymer stiffness and interconnections cause the cells containing suchhemoglobin to become rigid, thereby blocking the microcirculation. Although the central problem of sickle cell disease is rheological, no experiments are known that can relate rheologyat the cellular scale to the polymer formation that is its cause. A new technique has been developed to measure Rheology at microscopic scales that allow us to control polymerformation and characterize the formed domains at the same time. The created experimental apparatus and the established measurement techniques will be presented, results and theirimplication on our understanding of sickle hemoglobin rheology will be discussed. The unusual universality of sickle hemoglobin rigidity dependence on the amount of the formed polymer will be presented and discussed.
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Details
Title
A microrheological study of sickle hemoglobin polymerization
Creators
Mikhail N. Zakharov - DU
Contributors
Frank Ferrone (Advisor) - Drexel University (1970-)
Awarding Institution
Drexel University
Degree Awarded
Doctor of Philosophy (Ph.D.)
Publisher
Drexel University; Philadelphia, Pennsylvania
Resource Type
Dissertation
Language
English
Academic Unit
College of Arts and Sciences; Physics; Drexel University
Other Identifier
3075; 991014632699604721
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