Zare, F. | Search bioRxiv

bioRxiv2020

Therapeutic Communication Skills Training: An Effective Tool to Improve the Caring Behaviors of ICU Nurses

BackgroundCaring behaviors are crucial in intensive care units (ICU) because patients in these wards require high levels of care. Effective communication with patients is one of the most important factors in caring behaviors of nurses working in ICUs. Therefore, the aim of this study was to evaluate the effect of therapeutic communication skills training on the caring behaviors of ICU nurese. Materials and MethodsThis experimental pre-test/post-test study was carried out on 105 nurses working in ICUs of hospitals affiliated to Yazd University of Medical Sciences in Iran in 2019. Nurses were randomly assigned into control (52 nurses) and intervention (53 nurses) groups. A two-day therapeutic communication training workshop was conducted for the participants. Data were collected using demographic information questionnaire and caring behaviors questionnaire before and one month after the intervention. ResultsThe findings showed no significant difference between the control and intervention groups regarding the nurses caring behaviors in the pretest (P = 0.148). However, after implementation of the training program, a significant difference was observed in the mean scores of caring behaviors between the two groups. In the control group, the mean scores of caring behaviors decreased significantly after the intervention (P = 0.001); whereas, the mean scores of intervention group increased significantly after the intervention (P = 0.001). ConclusionAccording to the results, ICU nurses training in therapeutic communication skills had a positive effect on their caring behaviors. Therefore, we suggest the authorities prepare and implement educational packages of therapeutic communication skills as a coherent program for other nurses. As a result, the caring behaviors and the quality of cares can be improved for patients.

scientific communication and education↗

bioRxiv2019

High-yield Production of Recombinant Platelet Factor 4 Protein by Harnessing and Honing the Gram-negative Bacterial Secretory Apparatus

BackgroundPlatelet factor 4 is a cytokine released into the bloodstream by activated platelets and plays a pivotal role in heparin-induced thrombocytopenia etiology and diagnosis. Therefore, a sustainable source of recombinant PF4 with structural and functional similarity to its native form is urgently needed to be used in diagnostic procedures. To this end, a three-in-one primary construct was designed and custom synthesized based on the pET26b backbone from which three secondary constructs could be derived each capable of employing either type I, type II secretory or cytoplasmic pathways. Protein expression and secretion were performed in Escherichia coli BL-21 (DE3) and were confirmed by SDS-PAGE and Western blotting. To further enhance protein secretion, the effect of several controllable factors including IPTG, Triton X-100, Sucrose, and Glycine were individually investigated at first. In the next step, according to fractional factorial approach, the synergistic effect of IPTG, Triton X-100, and Glycine on secretion was further investigated. To ascertain the structure and function of the secreted recombinant proteins, Dynamic light scattering was utilized and confirmed rPF4 tetramerization and heparin-mediated ultra-large complex formation. Moreover, Raman spectroscopy was exploited to determine the rPF4 secondary structure. ResultsType II secretory pathway was proven to be superior over type I in case of rPF4 secretion into the extracellular milieu. Protein secretion mediated by Type II was enhanced to approximately more than 700 g/ml. Large quantities of native rPF4 up to 20 mg was purified upon a minor scale up to 40 ml of culture medium. Dynamic light scattering unveiled native rPF4 quaternary structure revealing the formation of tetramers having an average size of 10 nm and formation of larger complexes of approximately 100-1200 nm in size following heparin supplementation, implying proper protein folding, tetramerization, and antigenicity. Analysis of the Zeta potential on approximately 600 g/ml of rPF4 revealed a 98 mV positive charge which further confirms protein folding. Moreover, rPF4 secondary structure was determined to be 43.5% Random coil, 32.5% {beta}-sheet, 18.6 % -helix and 4.9 % Turn, which is in perfect agreement with the native structure. Conclusionour results indicate that the gram-negative type II bacterial secretory system holds a great promise to be employed as a reliable protein production strategy with favorable industrial application. However, further efforts are required to realize the full potential of secretory pathways regarding their application to proteins with distinct characteristics. O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=127 SRC="FIGDIR/small/830851v1_ufig1.gif" ALT="Figure 1"> View larger version (41K): org.highwire.dtl.DTLVardef@fd47fdorg.highwire.dtl.DTLVardef@8163c3org.highwire.dtl.DTLVardef@bcbb5eorg.highwire.dtl.DTLVardef@b145d5_HPS_FORMAT_FIGEXP M_FIG Graphical Abstract. rPF4 secretion mediated by type 2 secretory system. The pelB signal sequence directs protein export into the extracellular milieu through the SecYEG translocon complex in a process assisted by SecB chaperone. A) Indicates protein secretion before supplementation with additives and B) indicates secretion in the presence of additives. C_FIG

bioengineering↗