Effects of a multifaceted intervention in psychogeriatric patients: one-year prospective study.

OBJECTIVES: The aetiology of behavioural and psychological symptoms (BPSD) could be related to inadequate treatment in patients with dementia. The aim of this study was to determine how a multifaceted intervention based on a medication review and multidisciplinary follow-up could improve treatment and minimise risk in these patients. METHODS: A prospective interventional study was undertaken between July 2015 and July 2016 of patients with dementia admitted to control BPSD. Patients with previous psychiatric illness or palliative care were excluded. Prescription information was obtained from Aegerus and the Catalonia clinical record HC3. The intervention was conducted by a multidisciplinary team. The Medication Appropriateness Index (MAI) was used to assess the intervention. RESULTS: 65 patients (60% women, mean age 84.9±6.7 years) with mild-moderate cognitive impairment (mean 4.5±1.8), moderate-severe functional dependence (mean 43.8±23.9) and a high prevalence of geriatric syndromes and comorbidity were included in the study. 87.7% of the patients were taking ≥5 drugs (mean 9.0±3.1) and 38.5% were taking ≥10. Patients presented with BPSD values of 1.9±0.8 at admission. Common symptoms prompting admission were agitation (47.7%) and irritability (43.1%). A total of 175 drug-related problems (DRPs) were detected (2.97 per patient). Significant differences (p<0.001) were found between the MAI score at admission (4±4.6) and post-intervention (0.5±2.6). Most prevalent MAI criteria were related to interactions (40%), dosage (38.5%) and duplication (26.2%). 55 patients (84.6%) were taking anticholinergic drugs at admission (2.6±1.2 anticholinergic drugs per patient), and the post-intervention reduction was significant (p<0.016). CONCLUSIONS: The balance between effective treatment and safety is complex in these patients. Medication review in interdisciplinary teams is an essential component to optimise interventions and assessment of safety.

Interfacial properties of a synthetic peptide derived from hepatitis G virus E2 protein: interaction with lipid monolayers.

A useful approach to get information about the potential fusogenic ability of virus synthetic peptides is the study of its interfacial properties and subsequent study in mono- and bilayers. In this work, we have characterized by means of physicochemical tools (i.e. compression isotherms and surface activity) the sequence 267-284, LLGTEVSEVLGGAGLTGG, derived from the E2 structural protein of HGV/GBV-C. The adsorption of the peptide at the air/water interface was monitored by following the increase in surface pressure as a function of time at two different pH values: 5 and 7. Parameters such as surface excess or molecular area were calculated from the equation of Gibbs. The peptide showed a tendency to migrate to the surface of a saline-buffered solution. It formed stable monolayers at the air/water interface giving a compression isotherm with a shape consistent with that of some alpha-helical peptide conformations. Brewster angle microscopy (BAM) showed that through compression the peptide formed multilayers. The studies with lipid monolayers (DPMC, DMPC/DMPG, and DMPC/DMTAP) showed that the peptide interacts with all the lipids assayed producing a marked disrupting effect upon them. In these effects electrostatic interactions seem to have some participation.

Characterization of a putative fusogenic sequence in the E2 hepatitis G virus protein.

With the aim of better understanding the fusion process mediated by the envelope proteins of the hepatitis G virus (HGV/GBV-C), we have investigated the interaction with model membranes of two overlapping peptides [(267-284) and (279-298)] belonging to the E2 structural protein. The peptides were compared for their ability to perturb lipid bilayers by means of different techniques such as differential scanning calorimetry and fluorescence spectroscopy. Furthermore, the conformational behaviour of the peptides in different membrane environments was studied by Fourier-transform infrared spectroscopy and circular dichroism. The results showed that only the E2(279-298) peptide sequence was able to bind with high affinity to negatively charged membranes, to permeabilize efficiently negative lipid bilayers, to induce haemolysis, and to promote inter-vesicle fusion. This fusogenic activity could be related to the induced peptide conformation upon interaction with the target membrane.