Antip53 Autoantibody Detection in Automatic Glass Capillary Immunoassay Platform for Screening of Oral Cavity Squamous Cell Carcinoma The incidence of oral squamous cell carcinoma (OSCC), which is one of the most common cancers worldwide, has been increasing. Serum antip53 autoantibody is one of the most sensitive biomarkers for OSCC. Currently, the most commonly used method on clinical screening platforms is the enzymelinked immunosorbent assay, owing to its high specificity and repeatability. However, conducting immunoassays on 96well plates is typically time consuming, thereby limiting its clinical applications for fast diagnosis and immediate prognosis of rapidly progressive diseases. The present study performed immunoassays in glass capillaries of 1mm internal diameter, which increases the surface to volume ratio of the reaction, to shorten the time needed for immunoassay. The immunoassay was automated while using linear motorized stages and a syringe pump. The results indicated that, when compared with the 96well plate immunoassay, the glass capillary immunoassay decreased the reaction time from typical 120 min to 45 min, reduced the amount of reagent from typical 50 xc2xb5L to 15 xc2xb5L, and required only simple equipment setup. Moreover, the limit of detection for glass capillary antip53 autoantibody immunoassay was 0.46 ng mLxe2x88x921, which is close to the 0.19 ng mLxe2x88x921 value of the conventional 96well plate assay, and the glass capillary method had a broader detection range. The apparatus was used to detect the serum antip53 autoantibody concentration in clinical patients and compare its results with the conventional 96well plate method results, which suggested that both of the methods detect the same trend in the relative concentration of serum antip53 autoantibody in healthy individuals or patients with OSCC.

LabelFree Impedimetric Immunosensors Modulated by Protein ABovine Serum Albumin Layer for Ultrasensitive Detection of Salbutamol The sensing properties of immunosensors are determined not only by the amount of immobilized antibodies but also by the number of effective antigenbinding sites of the immobilized antibody. Protein A (PA) exhibits a high degree of affinity with the Fc part of IgG antibody to feasibly produce oriented antibody immobilization. This work proposes a simple method to control the PA surface density on gold nanostructure (AuNS)deposited screenprinted carbon electrodes (SPCEs) by mixing concentrationvaried PA and bovine serum albumin (BSA), and to explore the effect of PA density on the affinity attachment of antisalbutamol (SAL) antibodies by electrochemical impedance spectroscopy. A concentration of 100 xcexbcgmL PA and 100 xcexbcgmL BSA can obtain a saturated coverage on the 3mercaptoproponic acid (MPA)AuNSSPCEs and exhibit a 50% PA density to adsorb the amount of antiSAL, more than other concentrationvaried PABSAmodified electrodes. Compared with the randomly immobilized antiSALMPAAuNSSPCEs and the antiSALPA(100 xcexbcgmL):BSA(0 xcexbcgmL)MPAAuNSSPCE, the antiSALPA(100 xcexbcgmL): BSA(100 xcexbcgmL)MPAAuNSSPCEbased immunosensors have better sensing properties for SAL detection, with an extremely low detection limit of 0.2 fgmL and high reproducibility (u003c2.5% relative standard deviation). The mixture of PA(100 xcexbcgmL):BSA(100 xcexbcgmL) for the modification of AuNSSPCEs has great promise for forming an optimal protein layer for the oriented adsorption of IgG antibodies to construct ultrasensitive SAL immunosensors.