Discipline: Nanoscience or Materials Science
Subcategory: Nanoscience
Session: 4
Room: Forum
Nelson I. Molina Lara - University of Puerto Rico at Ponce
Co-Author(s): Jorge F. Pagán Román, University of Puerto Rico at Ponce, Puerto Rico, Ponce
Myoglobin is a single polypeptide chain protein that transports oxygen. This protein can be found in the heart and skeletal muscle tissues. When these tissues have an injury, Myoglobin is released into the bloodstream and then filtrated by the kidneys, which help remove Myoglobin from the body. High concentrations of Myoglobin in the kidneys could damage them, causing tubular necrosis and acute renal failure. An abnormally high concentration of Myoglobin in the urine could indicate a heart attack. A biosensor (an analytical device that combines a biological part with a physicochemical detector) could help to improve early prognosis and better diagnose diseases related to the presence of Myoglobin in body fluids with a faster and less expensive method, suppling a better quality of life. This study focuses on developing a Zinc Oxide Nano-Based Biosensor (ZnO-BS) for detecting Myoglobin in aqueous solutions.ZnO-BS was prepared by mixing zinc acetate/ethanol with hydrochloric acid/ethanol solutions by ultrasonication. Techniques such as High-Resolution Transmission Electron Microscopy (HRTEM), Photoluminescence (PL) spectroscopy, and Ultraviolet/Visible (UV/Vis) spectroscopy were used to characterize and analyze the interaction between the biosensor and Myoglobin in solution. HRTEM showed that the ZnO-BS nanoparticles had a spherical shape with a 5 nm approximate diameter. The PL Spectrum for ZnO-BS shows an excitation peak at 281 nm and an emission peak at 301 nm, but when mixed with Myoglobin, the intensity of the emission peak increased. UV/Vis spectrum for Myoglobin showed two signals. The absorption signal centered at approximately 410 nm is attributed to the heme group (active site of the Myoglobin). After mixing ZnO-BS and Myoglobin, the 410 nm signal of Myoglobin decreased and shifted in the presence of ZnO. It is plausible to state that the changes in absorbance and intensity show an interaction between ZnO-BS and Myoglobin active site. More studies are necessary to understand the ZnO-BS/Myoglobin interaction mechanism fully; future studies will focus on detecting the proteins at different concentrations and pH values.
Funder Acknowledgement(s): Institutional funds of the University of Puerto Rico at Ponce
Faculty Advisor: Dr. Milton E. Rivera Ramos, milton.rivera@upr.edu
Role: I took part in the synthesis and characterization of the ZnO nanoparticles, as well as studying the interaction with Myoglobin.