Assessing Students' Impressions of the Cultural Awareness of Pharmacy Faculty and Students.

Objective. To determine pharmacy students' impressions of their faculty's interactions with diverse student and patient populations. Methods. Three student focus groups were convened. Eighty-four page transcripts were coded, and emergent themes were identified by qualitative analysis. Results. Students defined diversity as multidimensional beyond traditional categories. Emergent themes were faculty awareness or lack of awareness of cultural diversity, disparate cultural perspectives and preferences within student groups, teaching/learning approaches to prepare students to be more culturally competent, and student group dynamics. First- and second-year students emphasized student-to-student interactions, while third- and fourth-year students emphasized a lack of preparation for the realities of contemporary practice based on instructional methods. Conclusion. Students perceived the majority of their pharmacy faculty to be culturally sensitive and aware, but microaggression and discrimination from faculty and student peers were experienced. Study implications can potentially improve curricular offerings, cultural awareness of faculty and students, and care to diverse patient populations

Charting the sequence-activity landscape of peptide inhibitors of translation termination

Apidaecin (Api), an unmodified 18-amino-acid-long proline-rich antibacterial peptide produced by bees, has been recently described as a specific inhibitor of translation termination. It invades the nascent peptide exit tunnel of the postrelease ribosome and traps the release factors preventing their recycling. Api binds in the exit tunnel in an extended conformation that matches the placement of a nascent polypeptide and establishes multiple contacts with ribosomal RNA (rRNA) and ribosomal proteins. Which of these interactions are critical for Api's activity is unknown. We addressed this problem by analyzing the activity of all possible single-amino-acid substitutions of the Api variants synthesized in the bacterial cell. By conditionally expressing the engineered api gene, we generated Api directly in the bacterial cytosol, thereby bypassing the need for importing the peptide from the medium. The endogenously expressed Api, as well as its N-terminally truncated mutants, retained the antibacterial properties and the mechanism of action of the native peptide. Taking advantage of the Api expression system and next-generation sequencing, we mapped in one experiment all the single-amino-acid substitutions that preserve or alleviate the on-target activity of the Api mutants. Analysis of the inactivating mutations made it possible to define the pharmacophore of Api involved in critical interactions with the ribosome, transfer RNA (tRNA), and release factors. We also identified the Api segment that tolerates a variety of amino acid substitutions; alterations in this segment could be used to improve the pharmacological properties of the antibacterial peptide