Risk Factors for Postoperative Puncture Site Bleeding after Interventional Treatment of Cerebrovascular Disease via Common Femoral Artery Puncture: A Retrospective Analysis of 710 Cases.

This study aimed to identify the risk factors associated with puncture site bleeding following percutaneous puncture of the common femoral artery during interventional treatment of cerebrovascular disease (CVD). A retrospective analysis was conducted on 710 patients who underwent interventional treatment for CVD via femoral artery puncture. Among them, 26 individuals (3.66%) experienced bleeding at the femoral artery puncture site. Binary logistic regression analysis was performed to identify risk factors for puncture site bleeding. The impact of salt bag compression on postoperative bleeding was evaluated in patients with intermediate to high bleeding risk scores. The bleeding group showed higher blood pressure, lower platelet counts, longer prothrombin time and activated partial thromboplastin time, as well as a higher prevalence of larger vascular sheath sizes and variations in the timing of anti-coagulant and anti-platelet therapy administration. The bleeding risk score was higher in the bleeding group, indicating its predictive value for bleeding risk. Higher bleeding risk score, unstable blood pressure, repeated puncture, and serious vascular conditions were significant risk factors for puncture site bleeding. Application of salt bag compression for a duration of 2 hours reduced postoperative puncture site bleeding in patients with intermediate to high bleeding risk scores. Our study identified several significant risk factors for puncture site bleeding after cerebral vascular intervention via femoral artery puncture, including the bleeding risk score, blood pressure, repeated puncture, and vascular conditions. Implementing salt bag compression as a preventive measure can help mitigate bleeding complications in these high-risk patients.

Multienzyme detection and in-situ monitoring of enzyme activity by bending CE using quantum dots-based polypeptide substrate.

Multienzyme detection and monitoring enzyme activity in situ are significant for the disease to diagnose. This study aims to develop a quantum dots (QDs)-based nanoprobe Cyanine5-DDDLEVLFQFPGLVPRGSGGHHHHHH-QDs (Cy5-LEVLVP-QD), which is able to detect two enzymes inside a bent capillary using CE. Cy5-LEVLVP and QDs were allowed to bind with each other through metal affinity interaction and then injected the Cy5-LEVLVP-QD complex into a capillary with different bends, followed by related enzyme that can cleave the Cy5-LEVLVP peptide. The fluorescence of Cy5 was excited by QDs due to Förster resonance energy transfer. By monitoring the peaks produced by the original Cy5-LEVLVP-QD complex and a significant fluorescence change, sensitive analysis of two different enzymes was conducted. Therefore, the novel approach of using capillaries with semicircular bends could prove particularly useful for enzyme investigating in disease.

Resolving quantum dots and peptide assembly and disassembly using bending capillary electrophoresis.

Despite the numerous techniques developed for the studying nanoparticle and peptide interaction nowadays, sensitive and convenient assay in the process of flow, especially to simulate the self-assembly of quantum dots (QDs) and peptide inflow in blood vessels, still remains big challenges. Here, we report a novel assay for studying the self-assembly of QDs and peptide, based on CE using a bending capillary. We demonstrate that the semicircles numbers of the bending capillary affect the self-assembly kinetics of CdSe/ZnS QDs and ATTO-D3 LVPRGSGP9 G2 H6 peptide. Moreover, benefitting from this novel assay, the effect of the position on the self-assembly has also been realized. More importantly, we also demonstrate that this novel assay can be used for studying the stability of the QDs-peptide complex inflow. We believe that our novel assay proposed in this work could be further used as a general strategy for the studying nanoparticle-biomolecule interaction or biomolecule-biomolecule interaction.

A CE-FL based method for real-time detection of in-capillary self-assembly of the nanoconjugates of polycysteine ligand and quantum dots.

Small molecules with free thiol groups always show high binding affinity to quantum dots (QDs). However, it is still highly challenging to detect the binding capacity between thiol-containing molecules and QDs inside a capillary. To conquer this limitation, a capillary electrophoresis with fluorescence detection (CE-FL) based assay was proposed and established to investigate the binding capacity between QDs and a poly-thiolated peptide (ATTO 590-DDSSGGCCPGCC, ATTO-C4). Interestingly, the results showed that interval time had a great influence on QDs and ATTO-C4 self-assembly, which can be attributed to longer interval time benefitting the binding of QDs to ATTO-C4. The stability assays on ATTO-C4-QD assembly indicated that high concentration of imidazole or GSH had a high capability of competing with the bound ATTO-C4, evidenced by dramatically dropping of S 625/S 565 ratio from 0.78 to 0.30 or 0.29. Therefore, all these results above suggested that this novel CE-FL based detection assay could be successfully applied to the binding studies between QDs and thiol-containing biomolecules.

A novel in-capillary assay for dynamically monitoring fast binding between antibody and peptides using CE.

Nowadays, despite numerous techniques available for the detection of antibody-peptide binding, sensitivity and detection limit inflow still remains a major challenge. Herein, we report a strategy for the detection of binding inflow of monoclonal anti-FLAG M2 antibody and 5,6-carboxyfluorescein-labeled FLAG tag in capillary. Antibody and peptides were sequentially injected into the capillary where they mixed and bound together. Capillary electrophoresis with fluorescence detection was employed to monitor the binding process, and the results showed that the efficacy of the antibody-peptide binding in capillary (in-capillary assay) is affected by the stoichiometry. Compared to the out-capillary assay, this novel assay showed different KD values and required a very short detection time, thus showing great potential for rapid detection as well as other applications. Additionally, our novel assay can be used to investigate the stability of the antibody-peptide complex. The addition of excess DYKDDDDK or TAMRA-DYKDDDDK, with similar binding priorities with M2, can leads to dissociation of the complex with a two-step mechanism including dissociation and association. We believed that our developed method can be extended to monitor wide range of other biomolecule interactions.

A novel monitoring approach of antibody-peptide binding using "bending" capillary electrophoresis.

Recently, the in-capillary electrophoresis assay has been applied to variety kinds of analyses owing to its multiple functional integrating features, including mixing of samples, reaction process of the mixtures, and the separation and detection in one capillary system. However, the micro-reactor still has its limitations to the currently available applications, especially the mixing step of the samples inside the capillary could not be well controlled automatically or manually. Herein, we have developed a novel capillary electrophoresis assay for the detection of antibody-peptide binding inside a bending capillary. Its efficacy was monitored using an anti-FLAG M2 antibody and its ligand conjugated with FAM dye (FAM-DYKD). The antibody and the peptide were mixed inside the bending capillary with sequential injections. It was found that the numbers of semi-circle on the capillary interfered by the antibody and peptide binding dynamic. Additionally, an online competition assay was performed, which further validated the efficacy of the bending capillary device on monitoring the dynamic binding between the antigen and antibody. In summary, our data suggests that the novel assay is a practical approach in monitoring the antibody-antigen complex formation at a nano-scale. It could be applied to detect any biomolecule-biomolecule interaction as a general strategy.