Senior Project Advisor
Clint Spiegel
Document Type
Project
Publication Date
Spring 2024
Keywords
Factor VIII, C2 Domain, Hydrophobicity, Membrane Binding, Protein Binding
Abstract
Factor VIII (FVIII) plays a crucial role in our body’s ability to prevent blood loss. This function comes from its ability to bind membranes and enhance catalytic function of other proteins. Membrane binding of FVIII relies on hydrophobic residues located at the lower C2 domain in a region named the PS head group. This study looks at how the enhancement of the hydrophobicity of this site can impact the protein binding ability to membranes. Specifically mutating the residues leucine at residue 2251 in the PS head group to phenylalanine, the study uses BLI instrumentation to determine whether this mutation can induce increased activity of FVIII. Results obtained find that this mutation reduces membrane binding capabilities despite its increase in hydrophobicity. These results are believed to be related to structural changes that may have occurred specifically to the PS binding region of the C2 domain.
Department
Chemistry
Recommended Citation
Jacobs, Mady, "Hydrophobicity of Factor VIII on Membrane Binding" (2024). WWU Honors College Senior Projects. 875.
https://cedar.wwu.edu/wwu_honors/875
Type
Text
Rights
Copying of this document in whole or in part is allowable only for scholarly purposes. It is understood, however, that any copying or publication of this document for commercial purposes, or for financial gain, shall not be allowed without the author’s written permission.
Language
English
Format
application/pdf