Plaque-forming self-assembling peptides are an important component in the study of neurodegenerative diseases, such as Alzheimer’s and Parkinson’s. Once the plaques are formed, it can be difficult to disassemble these structures chemically or enzymatically. MMP-9, a matrix metalloproteinase, is an enzyme produced in humans that is typically responsible for the cleavage of extracellular matrix, playing a role in developmental growth characteristics. Interestingly, it has been previously shown that MMP-9 can cleave self-assembling peptide substrates, including peptides in higher order oligomer structures. Our goal is to better understand how MMP-9 cleaves short self-assembling peptides based on the Aβ amyloid sequence. Using an Aβ amyloid derived peptide substrate, QKLVFFAEDK, the enzymatic activity and cleavage products of the proteolytic reaction will be examined. We will report upon the MALDI-TOF analysis of the cleavage products for characterization based upon the known mass fragments of the synthesized Aβ peptide substrate. HPLC analysis, in conjunction with a fluorescence assay, will be used to quantitatively assess the cleavage products. The information we gain about how MMP-9 can cleave these peptide structures can be beneficial for potential applications towards other large peptide structures that cannot easily be cleaved through traditional chemical means.

MMP-9 cleavage of self-assembling amyloid peptides

2019 Spring National Meeting

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