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In this study, we review the properties of three anionic detergents, sodium dodecyl sulfate (SDS), Sarkosyl, and sodium lauroylglutamate (SLG), as they play a critical role in molecular biology research. SDS is widely used in electrophoresis and cell lysis for proteomics. Sarkosyl and, more frequently, SDS are used for the characterization of neuropathological protein fibrils and the solubilization of proteins. Many amyloid fibrils are resistant to SDS or Sarkosyl to different degrees and, thus, can be readily isolated from detergent-sensitive proteins. SLG is milder than the above two detergents and has been used in the solubilization and refolding of proteins isolated from inclusion bodies. Here, we show that both Sarkosyl and SLG have been used for protein refolding, that the effects of SLG on the native protein structure are weaker for SLG, and that SLG readily dissociates from the native proteins. We propose that SLG may be effective in cell lysis for functional proteomics due to no or weaker binding of SLG to the native proteins.

Monoclonal antibodies to the soluble antigens or cell surface markers hold great promise as effective human therapeutics. One of the major disadvantages is its large size, which prevents efficient penetration into the target tissues. Smaller version of antibodies, which has only antigen binding sites, is extensively investigated. It becomes increasingly apparent, however, that these smaller fragments of antibodies are rather difficult to produce, as the normally efficient mammalian secretion system does not work well for these fragments. Thus, refolding of insoluble proteins produced in Escherichia coli is a method of choice, although such refolding is mainly based on trial-and-error experiment. Here we describe a novel refolding system using a new amino acid-based detergent, N-lauroyl-L-glutamate, and arginine. This detergent appears to readily dissociate from proteins below critical micelle concentration (CMC), while remaining effective in protein solubilization above CMC. Arginine suppresses protein aggregation when the detergent concentration was reduced below CMC. The interaction of the detergent and arginine with proteins, which play an important role in protein refolding, will be discussed in great length.

Three years after the outbreak of the coronavirus disease (COVID-19) pandemic, turnover among frontline nurses has increased. The participants of this study were nurses at two general hospitals in Ishikawa, Japan, receiving COVID-19 patients. An original self-report questionnaire was created based on previous research. The questionnaire was distributed to 400 nurses, and responses were received from 227 nurses (response rate: 56.8%). The factors influencing turnover intention at the facilities were having less time to relax (odds ratio [OR]: 2.88, 95% confidence interval [CI]: 1.12–7.41) and wanting to receive counseling (OR: 5.21, 95% CI: 1.30–20.91). As a strategy to prevent turnover, nurse managers should provide opportunities for nurses to receive counseling during normal working hours and pay particular attention to changes in nurses’ daily lives, such as changes in the time available for relaxation.