Participant comprehension and perspectives regarding the convenience, security, and satisfaction with teleconsent compared to in-person consent:A parallel-group pilot study among Danish citizens

BACKGROUND: Teleconsent via video conferencing enables decentralized trials with remote consent and has the additional benefit of allowing a real-time reaction to potential misunderstandings. However, participant acceptance of and satisfaction with teleconsent versus in-person consent processes are unknown. METHODS: We conducted a parallel-group pilot study to evaluate participant comprehension and perspectives regarding the convenience, security, and satisfaction with teleconsent compared to in-person consent among Danish citizens for a hypothetical research study. RESULTS: There were no statistically significant differences in perceptions of security or satisfaction between teleconsent and in-person consent arms. However, participants viewed teleconsent as more convenient than in-person consent, as no transportation was needed and the process was less time-consuming. Recruitment was also faster in the teleconsent arm, and more people dropped out of the in-person arm, citing difficulties with transportation and time. CONCLUSION: Decentralized clinical trials have been demonstrated to increase recruitment and enrollment rates, improve trial efficiency, and decrease dropout rates and trial delays. We add to this literature by suggesting that patients perceive teleconsent as similar to in-person consent, suggesting this is a feasible and acceptable substitution for in-person consent in multisite, decentralized trials. Future work should include patient perspectives from a larger, more diverse group of participants

Photonic activation of disulfide bridges achieves oriented protein immobilization on biosensor surfaces

Photonic induced immobilization is a novel technology that results in spatially oriented and spatially localized covalent coupling of biomolecules onto thiol-reactive surfaces. Immobilization using this technology has been achieved for a wide selection of proteins, such as hydrolytic enzymes (lipases/esterases, lysozyme), proteases (human plasminogen), alkaline phosphatase, immunoglobulins’ Fab fragment (e.g., antibody against PSA [prostate specific antigen]), Major Histocompability Complex class I protein, pepsin, and trypsin. The reaction mechanism behind the reported new technology involves “photonic activation of disulfide bridges,” i.e., light-induced breakage of disulfide bridges in proteins upon UV illumination of nearby aromatic amino acids, resulting in the formation of free, reactive thiol groups that will form covalent bonds with thiol-reactive surfaces (see Fig. 1). Interestingly, the spatial proximity of aromatic residues and disulfide bridges in proteins has been preserved throughout molecular evolution. The new photonic-induced method for immobilization of proteins preserves the native structural and functional properties of the immobilized protein, avoiding the use of one or more chemical/thermal steps. This technology allows for the creation of spatially oriented as well as spatially defined multiprotein/DNA high-density sensor arrays with spot size of 1 μm or less, and has clear potential for biomedical, bioelectronic, nanotechnology, and therapeutic applications