Improvement in quality of trauma care at non-tertiary hospitals in Ghana during on-hours and off-hours with a trauma intake form: A stepped-wedge cluster randomized trial.

BACKGROUND: We sought to determine the achievement of key performance indicators (KPIs) of initial trauma care at non-tertiary hospitals in Ghana during on-hours (8AM-5PM weekdays) compared to off-hours (nights, weekends, and holidays). We also sought to assess the effectiveness of a standardized trauma intake form (TIF) with built-in decision support prompts to improve care and to assess whether this effectiveness varied between on-hours and off-hours. METHODS: A stepped-wedge cluster randomized trial was performed with research assistants directly observing trauma care before and after introducing the TIF at emergency units of eight hospitals for 17.5 months. Differences in KPIs and mortality were assessed using multivariable logistic regression and generalized linear mixed regression. RESULTS: Management of 4,077 patients was observed; 1,126 (28 %) during on-hours and 2,951(72 %) during off-hours. At baseline, four of 20 KPIs were performed significantly more often during off-hours. TIF improved care during both on- and off-hours. Seventeen KPIs improved during on-hours and 18 KPIs improved during off-hours. After TIF, six KPIs were performed more often during on-hours, but differences, though significant, were small (1-5 %). Examples of KPIs which were performed more often during on-hours after TIF included: airway assessment (99 % for on-hours vs. 98 % for off-hours), evaluation for intra-abdominal bleeding (91 % vs. 87 %), and spine immobilization for blunt trauma (90 % vs. 85 %) (all p < 0.05). At baseline, mortality among seriously injured patients (Injury Severity Score >9) was higher during on-hours (27 %) compared to off-hours (17 %, p = 0.047). TIF lowered mortality for seriously injured patients during both on-hours (27 % before TIF, 8 % after, p = 0.027) and during off-hours (17 % before, 7 % after, p = 0.004). After TIF, mortality among seriously injured patients was equal between on- and off-hours (8 % vs. 7 %, NS). CONCLUSIONS: At baseline, KPIs of trauma care were slightly better during off-hours compared with on-hours, and mortality was lower among seriously injured patient during off-hours. A quality improvement initiative (the TIF) using built-in decision support prompts improved care strongly in both on- and off-hours and eliminated the mortality difference between on- and off-hours. Use of similar decision support prompts during initial trauma care should be promoted widely in other low- and middle-income countries.

Applications of chromatographic methods in metabolomics: A review.

Chromatography is a robust and reliable separation method that can use various stationary phases to separate complex mixtures commonly seen in metabolomics. This review examines the types of chromatography and stationary phases that have been used in targeted or untargeted metabolomics with methods such as mass spectrometry (MS) and nuclear magnetic resonance (NMR) spectroscopy. General considerations for sample pretreatment and separations in metabolomics are considered, along with the various supports and separation formats for chromatography that have been used in such work. The types of liquid chromatography (LC) that have been most extensively used in metabolomics will be examined, such as reversed-phase liquid chromatography and hydrophilic liquid interaction chromatography. In addition, other forms of LC that have been used in more limited applications for metabolomics (e.g., ion-exchange, size-exclusion, and affinity methods) will be discussed to illustrate how these techniques may be utilized for new and future research in this field. Multidimensional LC methods are also discussed, as well as the use of gas chromatography and supercritical fluid chromatography in metabolomics. In addition, the roles of chromatography in NMR- vs. MS-based metabolomics are considered. Applications are given within the field of metabolomics for each type of chromatography, along with potential advantages or limitations of these separation methods.

Immunoaffinity Chromatography for Protein Purification and Analysis.

Immunoaffinity chromatography (IAC) is a type of liquid chromatography that uses immobilized antibodies or related binding agents as selective stationary phases for sample separation or analysis. The strong binding and high selectivity of antibodies have made IAC a popular tool for the purification and analysis of many chemicals and biochemicals, including proteins. The basic principles of IAC are described as related to the use of this method for protein purification and analysis. The main factors to consider in this technique are also presented under a discussion of the general strategy to follow during the development of a new IAC method. Protocols, as illustrated using human serum albumin (HSA) as a model protein, are provided for the use of IAC in several formats. This includes both the use of IAC with traditional low-performance supports such as agarose for off-line immunoextraction and supports used in high-performance IAC for on-line immunoextraction. The use of IAC for protein analysis as a flow-based or chromatographic immunoassay is also discussed and described using HSA and a competitive binding assay format as an example. © 2023 Wiley Periodicals LLC. Basic Protocol 1: Off-line immunoextraction by traditional immunoaffinity chromatography Basic Protocol 2: On-line immunoextraction by high-performance immunoaffinity chromatography Basic Protocol 3: Competitive binding chromatographic immunoassay.

Analysis of drug interactions with serum proteins and related binding agents by affinity capillary electrophoresis: A review.

Biomolecules such as serum proteins can interact with drugs in the body and influence their pharmaceutical effects. Specific and precise methods that analyze these interactions are critical for drug development or monitoring and for diagnostic purposes. Affinity capillary electrophoresis (ACE) is one technique that can be used to examine the binding between drugs and serum proteins, or other agents found in serum or blood. This article will review the basic principles of ACE, along with related affinity-based capillary electrophoresis (CE) methods, and examine recent developments that have occurred in this field as related to the characterization of drug-protein interactions. An overview will be given of the various formats that can be used in ACE and CE for such work, including the relative advantages or weaknesses of each approach. Various applications of ACE and affinity-based CE methods for the analysis of drug interactions with serum proteins and other binding agents will also be presented. Applications of ACE and related techniques that will be discussed include drug interaction studies with serum agents, chiral drug separations employing serum proteins, and the use of CE in hybrid methods to characterize drug binding with serum proteins.

Approaches for the detection and analysis of antidrug antibodies to biopharmaceuticals: A review.

Antibody-based therapeutic agents and other biopharmaceuticals are now used in the treatment of many diseases. However, when these biopharmaceuticals are administrated to patients, an immune reaction may occur that can reduce the drug's efficacy and lead to adverse side-effects. The immunogenicity of biopharmaceuticals can be evaluated by detecting and measuring antibodies that have been produced against these drugs, or antidrug antibodies. Methods for antidrug antibody detection and analysis can be important during the selection of a therapeutic approach based on such drugs and is crucial when developing and testing new biopharmaceuticals. This review examines approaches that have been used for antidrug antibody detection, measurement, and characterization. Many of these approaches are based on immunoassays and antigen binding tests, including homogeneous mobility shift assays. Other techniques that have been used for the analysis of antidrug antibodies are capillary electrophoresis, reporter gene assays, surface plasmon resonance spectroscopy, and liquid chromatography-mass spectrometry. The general principles of each approach will be discussed, along with their recent applications with regards to antidrug antibody analysis.

Recent Advances in Supramolecular Affinity Separations: Affinity Chromatography and Related Methods.

Affinity chromatography is a technique that uses a stationary phase based on the supramolecular interactions that occur in biological systems or mimics of these systems. This method has long been a popular tool for the isolation, measurement, and characterization of specific targets in complex samples. This review discusses the basic concepts of this method and examines recent developments in affinity chromatography and related supramolecular separation methods. Topics that are examined include advances that have occurred in the types of supports, approaches to immobilization, and binding agents that are employed in this method. New developments in the applications of affinity chromatography are also summarized, including an overview on the use of this method for biochemical purification, sample preparation or analysis, chiral separations, and biointeraction studies.