Supplementary document for Switchable hybrid-order optical vortex lattice - 6909049.pdf

Experimental explanation of OV density in OV lattice and interferograms in Figs. 3 and

Ligand Replacement Approach to Raman-Responded Molecularly Imprinted Monolayer for Rapid Determination of Penicilloic Acid in Penicillin

Penicilloic acid (PA) is a degraded byproduct of penicillin and often causes fatal allergies to humans, but its rapid detection in penicillin drugs remains a challenge due to its similarity to the mother structure of penicillin. Here, we reported a ligand-replaced molecularly imprinted monolayer strategy on a surface-enhanced Raman scattering (SERS) substrate for the specific recognition and rapid detection of Raman-inactive PA in penicillin. The bis­(phenylenediamine)–Cu²⁺–PA complex was first synthesized and stabilized onto the surface of silver nanoparticle film that was fabricated by a bromide ion-added silver mirror reaction. A molecularly imprinted monolayer was formed by the further modification of alkanethiol around the stabilized complex on the Ag film substrate, and the imprinted recognition site was then created by the replacement of the complex template with Raman-active probe molecule <i>p</i>-aminothiophenol. When PA rebound into the imprinted site in the alkanethiol monolayer, the SERS signal of <i>p</i>-aminothiophenol exhibited remarkable enhancement with a detection limit of 0.10 nM. The imprinted monolayer can efficiently exclude the interference of penicillin and thus provides a selective determination of 0.10‰ (w/w) PA in penicillin, which is about 1 order of magnitude lower than the prescribed residual amount of 1.0‰. The strategy reported here is simple, rapid and inexpensive compared to the traditional chromatography-based methods

Combinatorial Drug Screening Based on Massive 3D Tumor Cultures Using Micropatterned Array Chips

The establishment and application of a generalizable three-dimensional (3D) tumor device for high-throughput screening plays an important role in drug discovery and cancer therapeutics. In this study, we introduce a facile microplatform for considerable 3D tumor generation and combinatorial drug screening evaluation. High fidelity of chip fabrication was achieved depending on the simple and well-improved microcontact printing. We demonstrated the high stability and repeatability of the established tumor-on-a-chip system for controllable and massive production of 3D tumors with high size uniformity. Importantly, we accomplished the screening-like chemotherapy investigation involving individual and combinatorial drugs and validated the high accessibility and applicability of the system in 3D tumor-based manipulation and analysis on a large scale. This achievement in tumor-on-a-chip has potential applications in plenty of biomedical fields such as tumor biology, pharmacology, and tissue microengineering. It offers an insight into the development of the popularized microplatform with easy-to-fabricate and easy-to-operate properties for cancer exploration and therapy

Funnel plot for PMI incidence to rule out publication bias.

<p>Funnel plot was generated using a fixed-effect model by Review Manager 5.2.0.</p

Characteristics of included studies.

<p>PCI = percutaneous coronary intervention; CK-MB = creatine kinase-MB; UNL = upper normal limit of normal; NSTE-ACS = non-ST-segment elevation acute coronary syndrome;</p><p>Characteristics of included studies.</p

Rapamycin induced mRNA and protein expression of KLF2 in HUVECs with thrombin.

<p>After stimulation with thrombin for 4 hours, rapamycin was added to HUVECs at concentrations of 2, 20, 200 and 2000 ng/ml for 24 and 48 hours. KLF2 was assessed by real-time PCR, western blot and immunofluorescence assays. Each bar represented the mean±SD (n = 6). Quantitative data for the PCR and western studies were shown graphically. A, rapamycin induced mRNA expression of KLF2 for 24 hours. B, rapamycin induced protein expression of KLF2 for 24 hours. C, rapamycin induced mRNA expression of KLF2 for 48 hours. D, rapamycin induced protein expression of KLF2 for 48 hours. Rapamycin enhanced the expression of KLF2 compared to stimulation with thrombin alone when the blood concentration of rapamycin was higher than 20 ng/ml (*p<0.05, **p<0.01 for rapamycin + thrombin vs thrombin alone). E, immunofluorescence staining of KLF2 in the nuclei of HUVEC, controls or treated with rapamycin. KLF2 was shown in red (left column). DAPI was used to stain cell nuclei (center column). The merged image was shown in the right column.</p

Rapamycin regulated mRNA and protein expression of eNOS in HUVECs.

<p>HUVECs were treated with rapamycin at concentrations of 2, 20, 200 and 2000 ng/ml for 24 and 48 hours. eNOS was assessed by real-time PCR and western blot. Each bar represented the mean±SD (n = 3). Quantitative data for the PCR and western studies were shown graphically. A, rapamycin reduced mRNA expression of eNOS for 24 hours. B, rapamycin reduced protein expression of eNOS for 24 hours. C, the mRNA expression of eNOS was induced after treating with rapamycin for 48 hours. D, the protein expression of eNOS was induced after treating with rapamycin for 48 hours. There was a significant decrease in mRNA and protein expression of eNOS after treating with rapamycin for 24 hours compared to control group (0 ng/ml). However, the expression of eNOS was enhanced by treating with rapamycin for 48 hours compared to control group. (*p<0.05, **p<0.01 for rapamycin vs control group).</p

Baseline characteristics among the four groups of subjects.

<p>BMI indicates body mass index; HCHO, hypercholesterolemia; DM, diabetes mellitus; CAD, coronary artery disease; MI, myocardial infarction; TC, total cholesterol; HDL-C, high density lipoprotein cholesterol; TG, triglyceride; FBG, fasting blood glucose; CR, serum creatinine; CK, creatine kinase; LVEF, left ventricle ejection fraction; CACS, coronary artery calcium score.</p><p>^b p<0.01 between the two groups.^a indicates a significant difference of p<0.05 between the S and the C group and </p><p>^d p<0.01 between the two groups.^c indicates a significant difference of p<0.05 between the M and the C group and </p><p>^f p<0.01 between the two groups.^e indicates a significant difference of p<0.05 between the H and the C group and </p

Coronary calcification was grouped as follows: spotty, length of calcium <3/2 of the vessel diameter and width <2/3 of the vessel diameter (A); medium, length of calcium ≥3/2 of the vessel diameter and width <2/3 of the vessel diameter or length of calcium <3/2 the vessel diameter and width ≥2/3 of the vessel diameter (B); and heavy, length of calcium burden ≥3/2 of the vessel diameter and width ≥2/3 of the vessel diameter (C).

<p>Coronary calcification was grouped as follows: spotty, length of calcium <3/2 of the vessel diameter and width <2/3 of the vessel diameter (A); medium, length of calcium ≥3/2 of the vessel diameter and width <2/3 of the vessel diameter or length of calcium <3/2 the vessel diameter and width ≥2/3 of the vessel diameter (B); and heavy, length of calcium burden ≥3/2 of the vessel diameter and width ≥2/3 of the vessel diameter (C).</p

Rapamycin regulated the activity of KLF2 in HUVECs with thrombin.

<p>A, After stimulation with thrombin for 4 hours, rapamycin was added to HUVECs at the concentration of 200 ng/ml for 2, 4, 8, 12, 24 and 48 hours. The activity of KLF2 was assessed by EMSA. B, After stimulation with thrombin for 4 hours, HUVECs were treated with rapamycin at concentrations of 2, 20, 200 and 2000 ng/ml for 24 hours. C, After stimulation with thrombin for 4 hours, HUVECs were treated with rapamycin at concentrations of 2000 ng/ml for 24 hours or rapamycin + anti-KLF2 antibody. Compared to the control group (thrombin alone), KLF2 bound to specific DNA sequences after treating with rapamycin of 2000 ng/ml for 24 hours. Specificity was shown by supershift binding using anti-KLF2 antibody. A 100-fold molar excess of cold competitor oligomers reduced the detection of all complexes.</p