Delivering information about medication assisted treatment to individuals who misuse opioids through a mobile app: a pilot study.

BACKGROUND: Digital therapeutic tools (e.g. mobile applications) can be accessible, low-cost interventions that counter misconceptions about medication assisted treatment (MAT) and/or improve deficits in MAT knowledge that are common barriers to treatment entry among individuals with opioid dependence. The purpose of this pilot study was to examine the preliminary effectiveness of a mobile application, 'uMAT-R', that includes health information about OUD recovery supported by science and MAT benefits. METHODS: Twenty-six adult participants with OUD recruited via social media completed all modules and pre/post-assessments within uMAT-R. McNemar's test was used to compare interest in treatment before and after completing the app, and paired t tests were used to compare MAT attitude scores before and after completing the modules within uMAT-R. RESULTS: Before viewing uMAT-R, 32% agreed/strongly agreed that they were interested in starting treatment to recover from opioid misuse, compared to 48% after completing uMAT-R. The average scores on the MAT attitudes scale and its Aid to Behavior Change subscale improved from before to after viewing uMAT-R. Among the participants, 88% felt that uMAT-R would be useful to consult when making decisions about recovery. CONCLUSIONS: Our encouraging pilot findings support the use of uMAT-R to help address the current opioid epidemic.

Role of Transmembrane Proteins for Phase Separation and Domain Registration in Asymmetric Lipid Bilayers.

It is well known that the formation and spatial correlation of lipid domains in the two apposed leaflets of a bilayer are influenced by weak lipid-lipid interactions across the bilayer's midplane. Transmembrane proteins span through both leaflets and thus offer an alternative domain coupling mechanism. Using a mean-field approximation of a simple bilayer-type lattice model, with two two-dimensional lattices stacked one on top of the other, we explore the role of this "structural" inter-leaflet coupling for the ability of a lipid membrane to phase separate and form spatially correlated domains. We present calculated phase diagrams for various effective lipid-lipid and lipid-protein interaction strengths in membranes that contain a binary lipid mixture in each leaflet plus a small amount of added transmembrane proteins. The influence of the transmembrane nature of the proteins is assessed by a comparison with "peripheral" proteins, which result from the separation of one single integral protein into two independent units that are no longer structurally connected across the bilayer. We demonstrate that the ability of membrane-spanning proteins to facilitate domain formation requires sufficiently strong lipid-protein interactions. Weak lipid-protein interactions generally tend to inhibit phase separation in a similar manner for transmembrane as for peripheral proteins.