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RUI: Mechanism of Biomolecule Stabilization in Solution by Tardigrade-specific CAHS Proteins

$306,783FY2024MPSNSF

Appalachian State University, Boone NC

Investigators

Abstract

With the support of the Chemistry of Life Processes (CLP) program in the Division of Chemistry, Dr. Brooke Christian of Appalachian State University will study the mechanism by which tardigrade-specific proteins can protect biomolecules from temperature-induced inactivation and degradation. Understanding how this protection occurs could shed light on how tardigrades survive elevated temperatures, which could allow the development of more robust formulations for commercial biomolecules such as enzymes and antibodies. These efforts will provide undergraduate students with specialized training in protein chemistry, which should increase competitiveness for graduate school and industry. The PI will also work with students in an undergraduate course-based undergraduate research experience (CURE) biochemistry lab and with Summer Ventures in Science and Mathematics, a program that allows high school students from across the state of North Carolina to participate in research. Cytoplasmic abundant heat soluble (CAHS) proteins are unique to tardigrades and are required for tardigrade desiccation survival, but their role in solution-phase stabilization is less well understood. This project will investigate three mechanisms of biomolecule protection: protein-protein interactions, stabilization of insulin and biomolecules other than proteins, and comparison of stabilization ability of various tardigrade proteins. Mechanisms of protection will be tested using a combination of protein activity assays under various conditions. These assays will include fluorescence spectroscopy, analytical ultracentrifugation, and western blotting. This project will investigate which CAHS proteins protect biomolecules best and seeks to determine optimal stabilization conditions to better understand how tardigrades survive elevated temperatures. This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.

View original record on NSF Award Search →