The Kv2.1 (KCNB1) channel is expressed in the cortex and hippocampus. Interaction between cysteine residues of the kv2.1 channel plays a role in the formation of disulfide bonds. Disulfide bond formation following oxidative stress suggests that cysteine interaction in voltage-gated K+ channel kv2.1 plays a key role in the oxidation of kv2.1. Previous research has shown that oxidation of potassium (K+) channels by reactive oxygen species (ROS) is a major factor in the loss of neuronal function [6]. The purpose of this study was to use cysteine-alanine mutations to prevent oxidation of K+ channel kv2.1. In this thesis, the anti-oxidant properties of the double mutant C73AC29A were investigated. The affects were observed using site-directed mutagenesis and the polymerase chain reaction (PCR). PCR was utilized to form a double mutant between C73A and C29A. SDS-Page and Western Blot analysis were used to analyze whether there was more or less oxidation in the double mutant C73AC29A compared to that of the kv2.1 control. The double mutant C73AC29A showed protective properties, showing less oxidation than the kv2.1 control when placed under oxidative stress. Findings suggest that C73AC29A could provide protection from oxidation-induced loss of function in the kv2.1 channel.
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Physiology and Integrative Biology
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Rutgers University Electronic Theses and Dissertations
Rutgers University. Graduate School - New Brunswick
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