Date of Award




Document Type

Master's Thesis

Degree Name

Master of Science (MS)


Department of Biological Sciences

Content Description

1 online resource (xii, 70 pages) : illustrations (some color)

Dissertation/Thesis Chair

Hua Shi

Committee Members

Robert Osuna, Jayanti Pande


Aptamer, Cancer, Chaperone, hsp27, hsp90, RNA, Heat shock proteins, Apoptosis, Oligonucleotides, Molecular chaperones

Subject Categories

Biology | Molecular Biology | Oncology


Hsp90 and Hsp27 are members of the heat shock protein family of chaperones that perform multiple roles in cellular maintenance through protein folding and inhibition of apoptosis. They are abundantly expressed in cells and are over-expressed during conditions of stress. Hsp90 requires ATP for its chaperone function while Hsp27 self-associates into higher order oligomers enclosing its substrate. Their ability to interact with other proteins or with themselves lies at the heart of their mechanisms. The specific consequences of each of their interactions on global cellular health have not yet been fully discovered. The sheer diversity of proteins that interact with Hsp90 and Hsp27 makes it harder to investigate their mechanisms through small molecule inhibitors or through small RNA silencing. Therefore, there is a growing need to use targeted approaches for dissecting the specificity and consequence of each of these interactions. This approach may also discover the structural changes that are necessary for chaperoning function of these two proteins. As a first step towards developing these tools, we have developed RNA aptamers for Hsp27 and Hsp90. In the future, these aptamers could possibly be used in-vivo to study the influence of these two chaperones on many aspects of cellular life including development, maintenance and death.