BYU

Abstract by Kevin Foote

Personal Infomation


Presenter's Name

Kevin Foote

Co-Presenters

None

Degree Level

Undergraduate

Co-Authors

None

Abstract Infomation


Department

Chemistry and Biochemistry

Faculty Advisor

Richard Watt

Title

Fe3+ Loading into Transferrin

Abstract

Transferrin (Tf) is the major serum iron transport protein; it binds iron with a binding constant of 1020. During inflammation, free iron is found in serum and causes oxidative stress by forming Reactive Oxygen Species (ROS). How does free iron form when TF’s binding constant is 1020? Our lab has shown that polymeric Fe3+ is not a substrate for TF and Fe3+ polymerizes with phosphate. We propose that serum albumin and citrate act to keep Fe3+ as a monomeric species for loading into TF. We used known UV/Vis iron loading assays and gel methods to evaluate iron loading into TF in the presence of molecules that stabilize monomeric Fe3+ [citrate, lactate, pyrophosphate] or molecules that polymerize Fe3+ [phosphate, glucose, sucrose]. Our results confirm our hypothesis that albumin and citrate help load iron into TF and molecules that trigger iron polymerization prevent TF iron loading and possibly form free iron in serum. Treatments that prevent iron polymerization will minimize free iron and ROS production and prevent oxidative stress during inflammation.