Pura Aerem: A Five-Stage Extension to Catalytic Converters Designed to Purify Gasses and Pollutants Exiting Gas-Powered Vehicles

Overview

Ambient air pollution contributes to a 7-million annual mortality rate, with gas-powered vehicles among the leading contributors. The current technology being used within gas-powered vehicles is the catalytic converter, converting gasses such as CO, HC, and NOX into CO2, H2O, N2, and other trace pollutants. The goal of this study was to improve catalytic converters, making the outputs less toxic. Pura Aerem was developed as a five-stage extension to catalytic converters designed to purify exhaust gasses exiting gas-powered vehicles. Pura Aerem uses diffusion-interception capture methods to reduce levels of particulate matter (PM), photoelectrochemical oxidation (PECO) technology to destroy trace gasses and pollutants, such as VOCs and O3, C60 Multi-Walled Buckypaper (MWBP) screening used to encapsulate CO2 particles, and an electrolysis chamber paired with a hydrogen fuel cell to utilize H2O for an alternative energy source. This study measured the levels of various gasses and pollutants in given samples over a 5-minute period from four environments. Altogether, Pura Aerem reduces Fine PM (FPM) and Coarse PM (CPM) by 99.275% and 99.587% (respectively), reduces CO2 by a minimum of 92.844%, reduces CO by nearly 100%, and increases O2 levels by approximately 744.444%. Chi-square tests were conducted, indicating that there was a significant FPM and CPM reduction correlated to the use of Pura Aerem (p=2.54×10-11, p=3.31×10-11–significance level of 0.05–respectively). Pura Aerem is a promising solution for future applications within internal combustion engines to reduce carbon emissions. KANSAS-NEBRASKA-OKLAHOMA The Effect of Palmitoylation on Drug Uptake Transporters in Human Hepatocytes Lydia Dorton Shawnee Mission East, Prairie Village, KS Principal Investigator: Dr. Bruno Hagenbuch, University of Kansas Medical Center The Organic Anion Transporting Polypeptide (OATP1B1) is a hepatic active transporter involved in the uptake of endogenous compounds and xenobiotic therapeutics. OATP1B1 is localized within lipid rafts in the cell membrane, frequently involved in an attachment process known as S-palmitoylation, a reversible post- translational modification. Post-translational modifications such as S-palmitoylation can affect the phenotype of the protein, at times massively affecting its ability to uptake substrates such as the xenobiotics and therapeutics it is responsible for transporting. Previous research has shown that single amino acid changes can greatly alter the uptake function and surface expression of proteins such as OATP1B1. The mutant C24A has been observed to affect uptake function when the surface function is normalized for both the mutant and the wild type. Uptake function significantly drops with the mutant compared to the wild type. The purpose of this study is to observe the effects of a single amino acid change at position 24 of OATP1B1 from cysteine to an alanine, specifically, if it de-palmitoylates OATP1B1, either partially or fully. By looking at concentrations of OATP1B1 and C24A in sucrose gradient fractions, it was observed that C24A shifts concentration into the higher numbered fractions. When graphed, this indicates that C24A may be partially de-palmitoylated, allowing it to move in the lipid rafts. This project falls into the category of Biomedical Sciences, subcategory of Pharmacology.

Competition history

• JSHS 2023 Category not listed

Resources

• National JSHS abstract book ↗

Related projects

Closest projects by meaning, across every fair and year in the corpus.