Impact of Patient Engagement and Social Determinants of Health on Care of Eosinophilic Gastrointestinal Disorders Patients.

ABSTRACT: The purpose of this study was to identify factors that influence eosinophilic gastrointestinal disorders (EGID) patients to switch gastroenterologists, assess the prevalence of social determinants of health (SDoH) in EGID patients, and the impact of SDoH on provider switching. 191 patients/caregivers participated in this cross-sectional, online study distributed through Patient Advocacy Groups. The 35-question survey took about 20 minutes to complete and was divided into three sections: demographics; 10 questions about provider switching; and nine-domain SDoH screen.Patients with EGIDs often switch providers, most commonly due to dissatisfaction with engagement in decision making. Additionally, these patients commonly have SDoH, some of which are associated with increased provider switching. Our results highlight the need to mindfully engage patients in decision-making and disease management. Providers also need to look beyond the "clinic space" and into SDoH. These low-cost/high-impact changes in provider behavior can promote continuity of care and patient engagement.

Folding of Gα Subunits: Implications for Disease States.

G-proteins play a central role in signal transduction by fluctuating between "on" and "off" phases that are determined by a conformational change. cAMP is a secondary messenger whose formation is inhibited or stimulated by activated Giα1 or Gsα subunit. We used tryptophan fluorescence, UV/vis spectrophotometry, and circular dichroism to probe distinct structural features within active and inactive conformations from wild-type and tryptophan mutants of Giα1 and Gsα. For all proteins studied, we found that the active conformations were more stable than the inactive conformations, and upon refolding from higher temperatures, activated wild-type subunits recovered significantly more native structure. We also observed that the wild-type subunits partially regained the ability to bind nucleotide. The increased compactness observed upon activation was consistent with the calculated decrease in solvent accessible surface area for wild-type Giα1. We found that as the temperature increased, Gα subunits, which are known to be rich in α-helices, converted to proteins with increased content of ß-sheets and random coil. For active conformations from wild-type and tryptophan mutants of Giα1, melting temperatures indicated that denaturation starts around hydrophobic tryptophan microenvironments and then radiates toward tyrosine residues at the surface, followed by alteration of the secondary structure. For Gsα, however, disruption of secondary structure preceded unfolding around tyrosine residues. In the active conformations, a π-cation interaction between essential arginine and tryptophan residues, which was characterized by a fluorescence-measured red shift and modeled by molecular dynamics, was also shown to be a contributor to the stability of Gα subunits. The folding properties of Gα subunits reported here are discussed in the context of diseases associated to G-proteins.