'iSupport' is an online psychoeducation and skills development intervention created by the World Health Organisation to support people with dementia. This project adapted iSupport for carers of people with rare dementias (iSupport RDC), creating a new resource to support the health and wellbeing of this underserved population. The adaptation involved three phases: (1) Co-design methods to generate preliminary adaptations; (2) Analysis of phase one findings informing adaptations to iSupport to develop; iSupport RDC; (3) Post-adaptation survey to ascertain participant agreement with the adaptations in iSupport RDC. Fourteen participants contributed, resulting in 212 suggested adaptations, of which 94 (92%) were considered practical, generalisable, and aligned with iSupport principles. These adaptations encompassed content and design changes, including addressing the challenges of rare dementias (PCA, PPA, LBD, and FTD). iSupport RDC represents a significant adaptation of the WHO iSupport intervention. Its tailored nature acknowledges the unique needs of people caring for someone with a rare dementia, improving their access to specialised resources and support. By extending iSupport to this population, it contributes to advancing dementia care inclusivity and broadening the understanding of rare dementias. A feasibility study is underway to assess iSupport RDCs acceptability, with prospects for cultural adaptations to benefit carers globally.

This work elucidates the mechanism involved in the effect of varying sterilization intensities on RDC thickening via comparative analysis of the changes in the composition and structure of RDC interfacial protein after storage at 4 °C and at 25 °C. The results showed that pasteurized RDCs (75 °C for 16 s, 90 °C for 5 min) and high-temperature sterilized RDCs (105 °C for 3 min, 115 °C for 7 min and 121 °C for 7 min) did not thicken during storage at 25 °C, and had lower viscosities and higher Ca2+ concentrations than those stored at 4 °C. Whey protein (WP) aggregates were found to have been adsorbed at the interface of high-temperature treated RDCs stored at 4 °C, leading to the aggregation of fat globules and, consequently, reversible thickening. However, high-temperature sterilized RDCs underwent into irreversible thickening at 10 d, 7 d and 3 d. This phenomenon was attributed to the large amount of heat-induced whey protein and κ-casein complex that was absorbed on the oil-water interface, with Ca2+ bonded to form bridging flocculation, which altered the secondary structure of the interfacial protein to one with increased β-sheet content and decreased random coil content.