A scoping review to identify barriers and facilitators of research participation among chiropractic faculty.

OBJECTIVE: To describe peer-reviewed literature on chiropractic faculty participation in research and identify important barriers and facilitators. METHODS: We conducted a scoping review using comprehensive searches of relevant databases from inception through November 2022. English language publications of any design were included, with search terms consisting of subject headings specific to each database and free text words related to chiropractic, faculty, and research. Primary and secondary reviewer teams performed article screening and data abstraction using Covidence software, with primary reviewers responsible for consensus. Data were entered into evidence tables and analyzed descriptively. RESULTS: A total of 330 articles were screened, with 14 deemed eligible including 8 cross-sectional/correlational studies and 6 narrative reviews/editorials. Article publication dates ranged from 1987 to 2017. No intervention studies were identified. Facilitators of chiropractic faculty research included research assignment as primary role, institutional culture promoting research, and dedicated release time. Barriers included teaching/clinic assignments, lack of incentives and mentorship, and teaching load. Qualitative results identified 5 domains impacting faculty research: demographics/professional roles; personal empowerment; research culture; institutional setting/policies; and research training. CONCLUSION: Our scoping review found a paucity of recently published articles on chiropractic faculty participation in research. Educational institutions building research capacity among chiropractic faculty must establish cultural environments where scholarship is expected, rewarded, and valued. Tangible support, such as research policies, resources, and space, advanced training, funding, and release time, must be available. Faculty are encouraged to build upon key facilitators, evaluate interventions to address barriers to chiropractic faculty research, and publish their results.

Automated enzyme-based diagonal capillary electrophoresis: application to phosphopeptide characterization.

Diagonal capillary electrophoresis is a form of two-dimensional capillary electrophoresis that employs identical separation modes in each dimension. The distal end of the first capillary incorporates an enzyme-based microreactor. Analytes that are not modified by the reactor will have identical migration times in the two capillaries and will generate spots that fall on the diagonal in a reconstructed two-dimensional electropherogram. Analytes that undergo enzymatic modification in the reactor will have different migration times in the second capillary and will generate spots that fall off the diagonal in the electropherogram. We demonstrate the system with immobilized alkaline phosphatase to monitor the phosphorylation status of a mixture of peptides. This enzyme-based diagonal capillary electrophoresis assay appears to be generalizable; any post-translational modification can be detected as long as an immobilized enzyme is available that reacts with the modification under electrophoretic conditions.

CE-MALDI interface based on inkjet technology.

An ink jet printer valve and a nozzle were used to deliver matrix and sample from an electrophoresis capillary onto a MALDI plate. The system was evaluated by the separation of a set of standard peptides. That separation generated up to 40 000 theoretical plates in less than 3 min. Detection limits were 500 amol for an ABI TOF-TOF instrument and 2 fmol for an ABI Q-TOF instrument. Over 70% coverage was obtained for the tryptic digest of alpha-lactalbumin in less than 2.5 min.

CE-microreactor-CE-MS/MS for protein analysis.

We present a proof-of-principle for a fully automated bottom-up approach to protein characterization. Proteins are first separated by capillary electrophoresis. A pepsin microreactor is incorporated into the distal end of this capillary. Peptides formed in the reactor are transferred to a second capillary, where they are separated by capillary electrophoresis and characterized by mass spectrometry. While peptides generated from one digestion are being separated in the second capillary, the next protein fraction undergoes digestion in the microreactor. The migration time in the first dimension capillary is characteristic of the protein while migration time in the second dimension is characteristic of the peptide. Spot capacity for the two-dimensional separation is 590. A MS/MS analysis of a mixture of cytochrome c and myoglobin generated Mascot MOWSE scores of 107 for cytochrome c and 58 for myoglobin. The sequence coverages were 48% and 22%, respectively.