Automatic Dispensing Pill Caddy for the Elderly

The report, Aging in the United States, finds that baby boomers who are at retirement age are in worse health compared with previous generations. More of them are living with chronic conditions such as high cholesterol, hypertension, diabetes, arthritis, and heart disease; all which require medication. The report also anticipates the number of people with dementia could nearly triple in the coming decades, resulting in senior adults requiring more assistance with daily activities. Our product intends to enhance the quality of life of the older adult population by providing a pill dispenser that creates convenience with alerts and notifications. This makes the dosage easily accessible to those with cognitive and other impairments, and helps these adults to live a healthier lifestyle all the while minimizing the stress involved and time needed to take their medication. The demographics for our customer base include those who are ages 65+ who have difficulty with memory, individuals who live with multiple diseases/chronic conditions, and elderly individuals who live independently and require regular assistance. We will reach our most relevant market by selling our product individually and also by providing access to hospitals, insurance companies, and care providers. Our product will add value to our end user’s life, is easily accessible for the elderly customers and can easily be changed with evolving technology.https://scholarscompass.vcu.edu/capstone/1190/thumbnail.jp

Catalytic activation of β-arrestin by GPCRs

β-arrestins are critical regulator and transducer proteins for G-protein-coupled receptors (GPCRs). β-arrestin is widely believed to be activated by forming a stable and stoichiometric GPCR-β-arrestin scaffold complex, which requires and is driven by the phosphorylated tail of the GPCR. Here we demonstrate a distinct and additional mechanism of β-arrestin activation that does not require stable GPCR-β-arrestin scaffolding or the GPCR tail. Instead, it occurs through transient engagement of the GPCR core, which destabilizes a conserved inter-domain charge network in β-arrestin. This promotes capture of β-arrestin at the plasma membrane and its accumulation in clathrin-coated endocytic structures (CCSs) after dissociation from the GPCR, requiring a series of interactions with membrane phosphoinositides and CCS-lattice proteins. β-arrestin clustering in CCSs in the absence of the upstream activating GPCR is associated with a β-arrestin-dependent component of the cellular ERK (extracellular signal-regulated kinase) response. These results delineate a discrete mechanism of cellular β-arrestin function that is activated catalytically by GPCRs