Perceptions of faculty in health care and social sciences on teaching international students

Background Increased cultural diversity of higher education (HE) students has created both learning opportunities and teaching challenges for vocational health care programs. An internationalized curriculum reflects sociocultural issues in professional practice and enhances intercultural competency amongst students. However, the literature is limited in seeking the key perspective of those delivering the curriculum. This study explores the awareness of health care teaching staff on issues related to internationalization, perceived responsibility in supporting international students, and teaching practices toward an inclusive curriculum. Methods An anonymous questionnaire was developed, consisting of different types of questions (Y/N, Likert scale, and multiple choice) with opportunities for free text on each main theme. The questionnaire was sent to all 205 staff members with a teaching remit at Cardiff University Schools of Postgraduate Medicine, Healthcare Sciences, Pharmacy, and Social Sciences. Key findings In all, 102 responses were received. Despite 70% of respondents feeling that the responsibility for an improved learning experience for international students lies beyond them—with the University, their School, or students themselves—inclusive teaching practices that consider cultural diversity are widely reported. Some individuals feel unprepared to teach international students, citing a lack of cultural knowledge and training. The proportion of international students is perceived as the most important aspect of internationalization. Other key components of national and institutional HE strategies, such as “internationalization abroad”, appear to be relatively unimportant. Findings from this study provide a basis for all higher education institutions educating health and social care professionals to reflect critically on the realities of engaging with the internationalization of vocational programs

Information required by community pharmacists to complete a Discharge Medicine Review for patients when they are discharged from hospital

Several studies have evaluated domiciliary medicines support services in terms of adherence, wastage and healthcare utilisation, yet few have considered patients’ risk of harm from their medicines. Such risk often manifests through non‐adherence or an inability to safely administer medicines; factors known to cause morbidity and mortality. The NPSA risk matrix (1) is widely used in practice to assess risks of harm in a variety of contexts; the risk score calculated is a composite of the likelihood and consequence of harm. This study concerns the novel application of the NPSA risk matrix to the recipients of a domiciliary medicines support service. The aim of the study was to determine the effect of the domiciliary medicines support service on patients’ medication related risk of harm

Peptides as therapeutic agents or drug leads for autoimmune, hormone dependent and cardiovascular diseases

Peptides regulate most physiological processes, mainly by binding to specific receptors located on the cell surface and inducing a series of signals, neurotransmissions or the release of growth factors. There has been a rapid expansion in the use of peptides as therapeutic agents after the 1960s, but a series of unfortunate side effects present in Phase I and II clinical studies combined with their low bioavailability, led to the introduction of the idea of peptidomimetics as alternative compounds that mimic the biological activity of peptides, while offering the advantages of increased bioavailability, biostability, bioefficiency, and bioselectivity. Since then new peptides with promising in vitro results, involving the monoclonal antibody expansion, as well as the newly launched research field for novel formulations for increasing peptides' bioavailability, redirected the interest on the peptide market. In this report we will highlight three areas where the use of peptides has shown promising results, with products that are either currently used as drugs or included into Phase III clinical studies

Structural requirements for binding of Myelin Basic Protein (MBP) Peptides to MHC II: effects on immune regulation

Confronting Multiple Sclerosis requires as an underlying step the manipulation of immune response through modification of Myelin Basic Protein peptides. The aim is to design peptidic or nonpeptidic molecules that compete for recognition of self-antigens at the level of antigen presentation. The rational approach is to substitute residues that serve as anchors for the T-Cell Receptor with others that show no binding at all, and those that serve as Major Histocompatibility Complex II anchors with others that present increased binding affinity. The resulting structure, hence, retains normal or increased MHC II binding properties, but fails to activate disease-inducing T-cells. This rational design can only be achieved by identifying the structural requirements for binding of the natural peptide to MHC II, and the anchor residues with their corresponding specific pockets in the binding groove. The peptide-MHC II complex then interacts with the TCR; thus, an additional way to trigger the desired immune response is to alter secondary anchor residues as well as primary ones. In this review, the structural requirements for binding of MBP peptides to MHC II are presented, as are the mechanism and key features for TCR recognition of the peptide-MHC II complex

Molecular dynamics at the receptor level of immunodominant myelin basic protein epitope 87-99 implicated in multiple sclerosis and its antagonists altered peptide ligands: Triggering of immune response

This work reports molecular dynamics studies at the receptor level of the immunodominant myelin basic protein (MBP) epitope 87–99 implicated in multiple sclerosis, and its antagonists altered peptide ligands (APLs), namely [Arg91, Ala96] MBP87–99 and [Ala91,96] MBP87–99. The interaction of each peptide ligand with the receptor human leukocyte antigen HLA-DR2b was studied, starting from X-ray structure with pdb code: 1ymm. This is the first such study of APL-HLA-DR2b complexes, and hence the first attempt to gain a better understanding of the molecular recognition mechanisms that underlie TCR antagonism by these APLs. The amino acids His88 and Phe89 serve as T-cell receptor (TCR) anchors in the formation of the trimolecular complex TCR-peptide-HLA-DR2b, where the TCR binds in a diagonal, off-centered mode to the peptide-HLA complex. The present findings indicate that these two amino acids have a different orientation in the APLs [Arg91, Ala96] MBP87–99 and [Ala91,96] MBP87–99: His88 and Phe89 remain buried in HLA grooves and are not available for interaction with the TCR. We propose that this different topology could provide a possible mechanism of action for TCR antagonism

Putative bioactive conformers of small molecules: A concerted approach using NMR spectroscopy and computational chemistry [Abstract]

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