20 µm Micro-LEDs Mass Transfer via Laser-Induced In Situ Nanoparticles Resonance Enhancement.

Ultrafast laser is expected as a promising strategy for micro-LEDs (µ-LEDs) transfer due to its inherent property of suppressing thermal effects. However, its ultrahigh peak power and the unclear transfer mechanism make its transfer quality and efficiency unsatisfactory. Here, the study reports the high-precision mass transfer of 20 µm fine-pitch µ-LEDs via in situ nanoparticles (NPs) resonance enhancement in burst mode ultraviolet picosecond laser irradiation. This technique suppresses the thermal melting effect and rapid cooling behavior of plasma by temporal modulation of the burst mode, generating NPs-induced resonance enhancement that accurately and controllable drives a single unit up to tens of thousands of µ-LEDs. The transfer of large µ-LED arrays with more than 180 000 chips is also demonstrated, showing a transfer yield close to 99.9%, a transfer speed of 700 pcs s-1, and a transfer error of <±1.2 µm. The transferred µ-LEDs perform excellent optoelectronic properties and enable reliable device operation regardless of complex strain environments, providing a reliable strategy for preparing broader classes of 3D integrated photonics devices.

Interactions between human hemoglobin subunits and peroxiredoxin 2.

Red blood cells (RBCs) are exposed to exogenous reactive oxygen species in the circulatory system. To this end, the interactions between the different hemoglobin (Hb) subunits and peroxiredoxin 2, which is a ubiquitous member of the antioxidant enzymes that also controls the cytokine-induced peroxide levels, were assessed. We predicted by the increment of diversity with quadratic discriminant analysis (IDQD) that peroxiredoxin2 (Prx2) could interact with the hemoglobin alpha, beta and gamma subunits but not with the delta subunit. Coimmunoprecipitation (co-IP), electrospray ionization quadrupole time of flight (ESI-Q-TOF) mass spectrometry, Western blotting and X-ray absorption fine structure (XAFS) spectroscopy were performed to verify these predictions. The results showed that Prx2 was a member of the beta-globin immunoprecipitating complex that existed in hemoglobin A, hemolysate-hemoglobin A, hemoglobin A-hemoglobin A2, hemolysate-hemoglobin A-hemoglobin A2 and hemoglobin A2 but not in hemolysate-hemoglobin A2. Adding Prx2 to hemoglobin A altered the second shell of iron embedded in hemoglobin A. Therefore, Prx2 interacts with hemoglobin A (Alpha2Beta2) and hemoglobin F (Alpha2Gamma2) but not with hemoglobin A2 (Alpha2Delta2).

Abnormal increased re-released Hb from RBCs of an intrahepatic bile duct carcinoma patient was detected by electrophoresis release test.

In this paper, the hemoglobin (Hb) re-released from red blood cells (RBCs) and whole blood of 7 carcinoma patients were studied by using electrophoresis release test (ERT), which was established by our lab. Among the 7 carcinoma patients, the re-released Hb was distinctively increased from an intrahepatic bile duct carcinoma patient during one-dimension isotonic ERT. Different from the others, the result of double-dimension Hb re-release of this intrahepatic bile duct carcinoma patient showed that not only HbA but also HbA2 could be re-released from both RBCs and whole blood. The result of isotonic & hypotonic ERT which was performed at room temperature showed that more Hb could be re-released from both RBCs and whole blood of the intrahepatic bile duct carcinoma patient than that of the normal control. After keeping the samples at 37°C for 1 hour, the re-released Hb from RBCs could still be found more than that of the normal control, but was disappeared completely from the whole blood sample. To our surprise, when the isotonic & hypotonic ERT was repeated 2 days later at 37°C, the re-released Hb from RBCs of the intrahepatic bile duct carcinoma patient was increased only in tube 4-6, and disappeared in the other tube. Further mechanism research work cannot be continued because of the patient's leave, but ERT is speculated to be a useful and effective technology to observe the physiological or pathological change of RBCs, blood or body in the future.

Molecular interactions of re-released proteins in electrophoresis of human erythrocytes.

Recently, we found that hemoglobin (Hb) could be re-released from live erythrocytes during electrophoresis release test (ERT). The re-released Hb displays single-band and multiple-band re-release types, but its exact mechanism is not well understood. In this article, the protein components of the single-band re-released Hb were examined. First, the re-released band of erythrocytes and the corresponding band of hemolysate, which was used as control, were cut out from starch-agarose mixed gel. Next, proteins were recovered from the starch-agarose mixed gel by freeze-thaw method. After condensing in a vacuum freeze drier, the samples were loaded onto a 5-12% SDS-PAGE. After electrophoresis, three protein bands (16, 28.9, and 29.3 kDa) emerged from the erythrocytes re-released Hb single-band (R-R), but only one band (29.3 kDa) emerged from the corresponding hemolysate control band (H-R). Finally, these bands were analyzed by MALDI-TOF MS. The results showed that these proteins were beta-globin (16 kDa), carbonic anhydrase 1 (CA1, 28.9 kDa), and carbonic anhydrase 2 (CA2, 29.3 kDa). Because CA2 exists in both erythrocytes re-released band and hemolysate control band, we conclude that the single-band re-released Hb is mainly composed of HbA and CA1. Studying the possible interaction between HbA and CA1 will help us further understand the in vivo function of Hb.

Interactions of hemoglobin in live red blood cells measured by the electrophoresis release test.

Electrophoresis release test (ERT) is the starch-agarose mixed gel electrophoresis of live red blood cells (RBCs). Mixed gel electrophoresis used to be one of the classic methods to isolate proteins, and in our laboratory, this technique is usually performed to isolate hemoglobins. Recently, combined with sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and liquid chromatography coupled with tandem mass spectrometry (LC/MS/MS), ERT has been used to study the interactions between hemoglobin and other proteins in live RBCs.

Interactions of hemoglobin in live red blood cells measured by the electrophoresis release test.

To elucidate the protein-protein interactions of hemoglobin (Hb) variants A and A(2), HbA was first shown to bind with HbA(2) in live red blood cells (RBCs) by diagonal electrophoresis and then the interaction between HbA and HbA(2) outside the RBC was shown by cross electrophoresis. The starch-agarose gel electrophoresis of hemolysate, RBCs, freeze-thawed RBCs and the supernatant of freeze-thawed RBCs showed that the interaction between HbA and HbA(2) was affected by membrane integrity. To identify the proteins involved in the interaction, protein components located between HbA and HbA(2) in RBCs (RBC HbA-HbA(2)) and hemolysate (hemolysate HbA-HbA(2)) were isolated from the starch-agarose gel and separated by 5-12% SDS-PAGE. The results showed that there was a ≈22 kDa protein band located in the RBC HbA-HbA(2) but not in hemolysate HbA-HbA(2). Sequencing by LC/MS/MS showed that this band was a protein complex that included mainly thioredoxin peroxidase B, α-globin, δ-globin and ß-globin. Thus, using our unique in vivo whole blood cell electrophoresis release test, Hbs were proven for the first time to interact with other proteins in the live RBC.

RBC electrophoresis with discontinuous power supply - a newly established hemoglobin release test.

In this paper, we aimed to introduce a newly established red blood cells (RBCs) electrophoresis method hemoglobin release test (HRT) and tried to determine its significance. Human blood samples from beta-thalassemia patients and healthy controls were analyzed with HRT, which was carried out on starch-agarose mixed gel. First, the whole blood samples were electrophoresed for 2 h, then paused for 15 min and ran for 15 min by turns. This "pause-run-pause" experiment was performed for several turns and the total electrophoresis time lasted for about 6 h. The results showed that some other hemoglobin (Hb) components were released from the origin of each sample during the HRT, and the samples from beta-thalassemia patients released more Hb than the healthy controls. This finding demonstrates that Hb may exist differently associated in RBCs, and it may have an important theoretical and clinical significance in Hb and RBC research.