Aya
Yangurazova
Sponsor: Christopher Simmons, Ph.D. Food Science & Technology Plastics are heavily used in agriculture; however they pose a risk to soil health due to fragmentation or improper disposal. Bioplastics have been proposed as a more sustainable alternative to plastics, however they need to retain the same properties as their counterparts in order to be used in practice. We used microcosm systems to simulate field biosolarization conditions to evaluate whether bioplastic can produce similar responses observed under conventional plastics. In order to test this hypothesis, we used heat-sealed microcosms to simulate biosolarization in incubators with various different types of commercial bioplastic and plastic films to determine whether similar biosolarization responses can be observed. Electrical conductivity (EC), soil pH, germination index, and biological organic acids were measured to compare the effectiveness of biosolarization across treatments. Under biosolarization conditions, soils exhibited consistently higher phytotoxic responses compared to solarized or unamended systems, with Mater-Bi bioplastic performing similarly to conventional polyethylene. Soil pH remained relatively stable but slightly lower than in solarized soils. EC increased under biosolarization, both in plastic and bioplastic covered soils, indicating substantial changes in soil ionic environments. Together, these findings suggest bioplastic treatments produced phytotoxic and chemical responses comparable to those observed under conventional plastic, indicating similar biosolarization effectiveness. Characterizing C-peptide Aggregation Using Single-Molecule, Super-Resolution Fluorescence Microscopy
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Aya Yangurazova
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Protein aggregation is associated with over 25 diseases, including Alzheimer's disease, Parkinson's disease, and type 2 diabetes. Aggregation occurs when misfolded proteins "stick" to one another and accumulate into larger species to form insoluble fibrils and amorphous aggregates. Characterizing the factors that influence protein aggregation is crucial for understanding disease mechanisms and developing treatments. In our experiments, we have examined the effect of chemical environment on the formation of C-peptide aggregates at the nanoscale using single- molecule, super-resolution fluorescence microscopy. C-peptide, a 31-amino acid peptide produced by pancreatic β-cells alongside insulin, maintains important physiological roles, and appears to interact with the aggregation-prone proteins insulin and islet amyloid polypeptide. We have found that aggregate type (fibrillar vs. amorphous), size, and heterogeneity depend on peptide concentration, pH, surfactants, metal ion concentration, and temperature. In combination with structural information from circular dichroism, super-resolution fluorescence microscopy measurements allow us to build a detailed understanding of C- peptide aggregates at the molecular level, providing insight into both biological function and aggregation mechanisms. This study of physiologically relevant peptides may also inform our understanding of aggregation processes and mechanisms in other protein aggregate diseases, providing a pathway for future research and cures. A Revolution of Consciousness: The 2026 Pilipinx Youth Conference Himagsikan: To Know Is to Survive Nicole Yanuaria
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UC Davis / Chemistry / 2026
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Aya Yangurazova