IRB Consent Guidelines: Potential Barriers to Diversity in Research.

Despite initiatives aimed at improving study participation and inclusion among ethnic and racially minoritized and marginalized populations, participation remains low. While necessary to ensure ethical practice in human participant research, certain Institutional Review Board (IRB) guidelines may introduce additional barriers in research involving these populations. This work outlines guidelines pertaining to consent translation for non-English speaking populations and offers discussion on a greater emphasis for more inclusive methods for marginalized communities. The University of Wisconsin's IRB approved alternative oral consent processes after the community partner determined that standard translation processes would be inefficient. Researchers used translated consent materials for four different ethnic groups (Hmong, Karen, Karenni, and Burmese). We provided recorded consents in each respective language to participants before study participation and obtained verbal consent prior to study participation at the study location. We experienced time and resource constraints in both access to translators and the consent-translation process itself. Furthermore, many participants were unable to read in their native language making standard written consent processes both difficult and impractical. Oral discussion and verbal consent processes were efficient. Adjustments to consent-related guidelines may prevent and eliminate time and resource-related barriers in consent processes. In eliminating such barriers, subsequent improved efficiency in both study design and study promotion areas can work to better promote diversity in research among populations that emphasize oral language and in instances where literacy rates in written non-English language may be lower.

Protein Immobilization on Gold Nanoparticles: Quantitative Analysis.

Conjugation of gold nanoparticles (AuNPs) with biologically relevant molecules underpins many applications in medicine and biochemistry. Immobilization of functional proteins on AuNPs often affects protein structure and function. Such effects are protein dependent and require thorough investigation using suitable quantitative tests. Good experimental design and the use of a comprehensive set of control samples are essential when characterizing the consequences of protein immobilization and its effect on protein structure and function. However, traditional approaches to making control samples, that is, immobilized protein versus protein in solution in absence of any nanoparticles, do not provide sufficiently identical reaction conditions and complicate interpretation of the results. Accurate quantification of protein conjugation to AuNPs and ensuring complete removal of unconjugated protein remain the two key challenges in such functional assays. This report describes a simple and straightforward procedure allowing for quantitative analysis of protein conjugation to AuNPs. The principles are illustrated using fluorescence and circular dichroism measurements, and can be applied to other analytical techniques or be adapted with minor modifications for use with other proteins.