Rama, Silvana Apryl (2024) The structure-function relationship of Multimerin-1, a platelet protein. Masters by Research thesis (MSc), Manchester Metropolitan University.
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Abstract
Multimerin-1 (MMRN1), a large mammalian glycoprotein, has emerged as a pivotal player in various physiological processes, including blood coagulation, angiogenesis, and vascular haemostasis. As a novel target for pathogenic proteins, such as Extracellular fibrinogen binding protein (Efb) from Staphylococcus aureus and Vacuolating cytotoxin A (VacA) from Helicobacter pylori and potential as a cancer biomarker with its differential expression monitored across various cancer types, positions MMRN1 as a compelling candidate for further exploration. However, little is known about MMRN1 structure-function relationship and how it links to its physiological function. This thesis aimed to explore the MMRN1 domain's structural characteristics, functional attributes, and molecular interactions by employing biochemical assays to explore the expression and cloning conditions that enhance its soluble production. The analysis of one construct had been successfully confirmed while discussing major obstacles and optimisation for future exploration. By investigating domain-specific growth conditions, this will inform novel studies surrounding their structure, function, and interactions with other proteins to provide insight into MMRN1's role in health and disease and potential implications in diagnostics and therapeutics.
Impact and Reach
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