Structural Comparison of the Matrix Metalloproteinase Proenzymes Using Microfluidic Modulation Spectroscopy

Matrix Metalloproteinases (or MMPs) are a class of proteases responsible for the degradation of extracellular matrix (ECM) proteins. Overexpression of certain MMPs is linked to various pathological disorders, including cancer, multiple sclerosis, and strokes. More recently, elevated MMPs have been identified in COVID-19 patients due to their essential roles in lung physiology. Consequently, there is significant research interest in utilizing MMPs as biomarkers to predict the severity of COVID-19 and developing inhibitors for targeted treatment strategies in severe cases of the disease. Therefore, understanding the structural variations among different MMPs is essential for advancing this research goal. Various MMPs play distinct roles in ECM tissue remodeling. For example, MMP-8, also known as collagenase, digests collagens, while MMP-2 and MMP-9, referred to as gelatinases A and B, respectively, target gelatins. All these MMPs have shown increased expression levels in COVID-19 patients. Thus, investigating both the commonalities and differences in the structure of these MMPs will prove invaluable in this context.