Arden Clauss

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Arden is a rising senior chemistry major at Carleton College. He greatly values the time he spends with his peers exploring scientific understanding, and is particularly interested in physical and analytical chemistry and biochemistry and their applications in advancing society. As part of the Amgen Scholars Program at UCLA, Arden is conducting research in the lab of Dr. José Rodríguez in the Department of Chemistry and Biochemistry. The Rodríguez lab studies structural biology with computational, biochemical, and biophysical approaches using imaging methods such as electron microscopy, x-ray diffraction, and electron diffraction. Arden is using these diffraction methods to explore structural aspects of binding in enzyme inhibition. Papain is a cysteine protease used as a model system for numerous analogous enzymes including the particularly relevant PLpro domain of Nsp3 from SARS-CoV-2, which is vital for viral replication. Inhibition of papain is possible with small molecules such as E64 that irreversibly bind the thiol group at the active site characteristic of these enzymes. Examining binding of E64 derivatives is of interest for selective inhibition of cysteine proteases, which has potential as a therapeutic tool in targeting viral and neurodegenerative disease pathways. Arden would like to thank his mentors Professor Rodríguez and Niko Vlahakis for their invaluable guidance, as well as UCLA and the Amgen Scholars Program for providing him with this opportunity to grow as a scientist.

Arden is a rising senior chemistry major at Carleton College. He greatly values the time he spends with his peers exploring scientific understanding, and is particularly interested in physical and analytical chemistry and biochemistry and their applications in advancing society.

As part of the Amgen Scholars Program at UCLA, Arden is conducting research in the lab of Dr. José Rodríguez in the Department of Chemistry and Biochemistry. The Rodríguez lab studies structural biology with computational, biochemical, and biophysical approaches using imaging methods such as electron microscopy, x-ray diffraction, and electron diffraction. Arden is using these diffraction methods to explore structural aspects of binding in enzyme inhibition. Papain is a cysteine protease used as a model system for numerous analogous enzymes including the particularly relevant PLpro domain of Nsp3 from SARS-CoV-2, which is vital for viral replication. Inhibition of papain is possible with small molecules such as E64 that irreversibly bind the thiol group at the active site characteristic of these enzymes. Examining binding of E64 derivatives is of interest for selective inhibition of cysteine proteases, which has potential as a therapeutic tool in targeting viral and neurodegenerative disease pathways.

Arden would like to thank his mentors Professor Rodríguez and Niko Vlahakis for their invaluable guidance, as well as UCLA and the Amgen Scholars Program for providing him with this opportunity to grow as a scientist.