Galectin-1 (Gal-1) is a protein that binds carbohydrates with β-galactoside linkages. Through this binding, Gal-1 exerts a variety of immune modulatory effects. Gal-1, however, has a high propensity to oxidative inactivation. Here, we demonstrate that Gal-1 cysteine residues can be altered by alkylation with iodoacetamide. This alteration inhibits oxidation of Gal-1 as measured by column affinity binding and HL-60 cell agglutination. Additionally, we show that Gal-1 possesses antimicrobial properties and can directly kill Providencia alcalifaciens O5 (PAO5), a pathogenic bacteria species known to cause traveler’s diarrhea. Furthermore, we demonstrate that oxidation regulates Gal-1’s antimicrobial properties as alkylated Gal-1 exhibits stronger bactericidal activity despite similar binding potential. We also studied the oxidation of Gal-1 to understand structural changes between reduced and oxidized Gal-1. While we do not presently have a crystal structure of oxidized Gal-1, we successfully optimized oxidation conditions such that we can produce purely oxidized monomeric Gal-1. We intend to use this optimization to make crystals of oxidized Gal-1 and elucidate atomic level structural changes of Gal-1 oxidation.
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About this Honors Thesis
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|File download under embargo until 24 May 2021||2019-04-23 13:25:49 -0400||File download under embargo until 24 May 2021|