Objectives: Blood microsampling, particularly dried blood spots (DBSs), is an attractive minimally-invasive approach that is well suited for home sampling and predictive medicine associated with longitudinal follow-up of the elderly. However, in vitro diagnostic quantification of biomarkers from DBS poses a major challenge. Clinical mass spectrometry can reliably quantify blood proteins in various research projects. Our goal here was to use mass spectrometry of DBS in a real-world clinical setting and compared it to the standard immunoassay method. We also sought to correlate DBS mass spectrometry measurements with clinical indices. Methods: A clinical trial of diagnostic equivalence was conducted to compare conventional venous samples quantified by immunoassay and DBSs quantified by mass spectrometry in an elderly population. We assayed three protein biomarkers of nutritional and inflammatory status: prealbumin (transthyretin), C-reactive protein, and transferrin. Results: The analysis of DBSs showed satisfactory variability and low detection limits. Statistical analysis confirmed that the two methods give comparable results at clinical levels of accuracy. In conclusion, we demonstrated, in a real-life setting, that DBSs can be used to measure prealbumin, CRP and transferrin, which are commonly used markers of nutritional status and inflammation in the elderly. However, there was no correlation with patient frailty for these proteins. Conclusions: Early detection and regular monitoring of nutritional and inflammatory problems using DBS appear to be clinically feasible. This could help resolve major public health challenges in the elderly for whom frailty leads to serious risks of health complications.

Management of lateral incisor agenesis is a real challenge and needs a strong collaboration between surgical, aesthetic, and orthodontic dentistry. This case report managed upper lateral incisor agenesis with an orthodontic treatment leading to open spaces and placement of cuspids in lateral incisor area to avoid implant placement in maxillary anterior region. Temporary rehabilitation phase, using resin injected tray and removable partial denture, has been placed to maintain mesiodistal dimensions and restore aesthetic during pre‐implant analysis and osseointegration. Once osseointegration was fully obtained, keratinized tissue augmentation has been obtained using connective tissue graft. Then, temporary implant fixed crowns allowed soft tissue modeling during interim rehabilitation. Finally, screw‐retained permanent crowns were placed to fully restore aesthetic and function. This case goal was to optimize final results and reach patient complete satisfaction using orthodontic treatment combined with implant rehabilitation, and coupled with interdisciplinary management and well‐time sequencing treatment.

Blood microsampling combined with large panels of clinically relevant tests are of major interest for the development of home sampling and predictive medicine. The aim of the study was to demonstrate the practicality and medical utility of microsamples quantification using mass spectrometry (MS) in a clinical setting by comparing two types of microsamples for multiplex MS protein detection. In a clinical trial based on elderly population, we compared 2 µL of plasma to dried blood spot (DBS) with a clinical quantitative multiplex MS approach. The analysis of the microsamples allowed the quantification of 62 proteins with satisfactory analytical performances. A total of 48 proteins were significantly correlated between microsampling plasma and DBS (p < 0.0001). The quantification of 62 blood proteins allowed us to stratify patients according to their pathophysiological status. Apolipoproteins D and E were the best biomarker link to IADL (instrumental activities of daily living) score in microsampling plasma as well as in DBS. It is, thus, possible to detect multiple blood proteins from micro-samples in compliance with clinical requirements and this allows, for example, to monitor the nutritional or inflammatory status of patients. The implementation of this type of analysis opens new perspectives in the field of diagnosis, monitoring and risk assessment for personalized medicine approaches.

Background: The differential diagnosis of α-synucleinopathies, including Parkinson’s disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA), is challenging due to overlapping clinical features and the current lack of reliable biomarkers. The primary diagnostic approach remains clinical, underscoring the need for objective biomarkers that can distinguish between these diseases. This study profiles α-synuclein peptides in plasma to explore potential disease-specific patterns. Methods: We developed a targeted mass spectrometry-based assay to profile α-synuclein in plasma samples from PD (n=82), DLB (n=32), MSA (n=8), and controls (n=21). The assay quantifies non-modified peptides specifically derived from the N-terminus and NAC domain, regions implicated in aggregate formation, to assess potential disease-specific peptide patterns. Results: No significant differences in peptide levels were observed between the disease groups, indicating consistent N-terminus and NAC domain profiles among α-synucleinopathies. However, a peptide within the NAC domain showed distinct patterns in MSA compared to other groups, which may reflect unique pathological processes. Conclusions: This study provides the first blood-based assessment of α-synuclein peptide profiles, establishing a basis for future research into α-synucleinopathies. Refining the assay to include post-translationally modified peptides may enhance understanding of disease mechanisms and improve biomarker development.