ArticleThe protein journal2026
Tryptophan-Mediated Sodium Dodecyl Sulfate Binding to Proteins.
Article in The protein journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Authors and funding
3 authors.
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Abstract
Sodium dodecyl sulfate (SDS) is widely used in protein research. Micellar binding of SDS is accepted as a major mechanism of SDS binding to proteins. Here, we investigated SDS-protein interactions using near-UV circular dichroism (CD), fluorescence spectroscopy, and SDS-gel electrophoresis. Bovine serum albumin (BSA), IgG, and lysozyme showed unfolding by SDS without heating or disulfide reduction as determined by SDS-gel electrophoresis. Near-UV CD and fluorescence spectroscopy showed changes in local structures surrounding tryptophan residues upon addition of 0.05-1% SDS. The fluorescence emission was blue-shifted by SDS, indicating that SDS creates more hydrophobic environments for the fluorescent tryptophan residues. We propose that, as one of the modes of SDS binding, both stoichiometric and cluster-like SDS binding occur around the fluorescent tryptophan residues, leading to changes in aromatic CD and fluorescence spectra.
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Registered trials
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