Datasheet1_Hemodynamics of the VenusP Valve System™—an in vitro study.docx

This study aims to evaluate the fluid dynamic characteristics of the VenusP Valve System™ under varying cardiac outputs in vitro. A thorough hemodynamic study of the valve under physiological cardiac conditions was conducted and served as an independent assessment of the performance of the valve. Flow fields downstream of the valve near the pulmonary bifurcation were quantitatively studied by two-dimensional Particle Image Velocimetry (PIV). The obtained flow field was analyzed for potential regions of flow stasis and recirculation, and elevated shear stress and turbulence. High-speed en face imaging capturing the leaflet motion provided data for leaflet kinematic modeling. The experimental conditions for PIV studies were in accordance with ISO 5840-1:2021 standard, and two valves with different lengths and different orientations were studied. Results show good hemodynamics performance for the tested valves according to ISO 5840 standard without significant regions of flow stasis. Observed shear stress values are all well below established hemolysis limits.</p

Simple Means for Fractionating Protein Based on Isoelectric Point without Ampholyte

In this paper, we develop a simple electrokinetic means for fractionating protein samples according to their p<i>I</i> values without using ampholytes. The method uses inexpensive equipment, and its consumables are primarily ammonium acetate buffers. A key component of its apparatus is a dialysis membrane interface that eliminates electrolysis-caused protein oxidation/reduction and constrains proteins in the desired places. We demonstrate its feasibility for fractionating standard proteins and real-world samples. With the elimination of ampholytes, we can analyze the fractionated proteins directly by a matrix assisted laser desorption/ionization time-of-flight mass spectrometer. Important experimental parameters are also discussed in order to obtain good fractionation results

Protein Translocation through a MoS₂ Nanopore:A Molecular Dynamics Study

Single-molecule protein sequencing is essential for a wide range of research and application fields, where the recently emerging 2D nanopores have open unprecedented possibilities. The protein translocating through a 2D nanopore plays vital roles in the nanopore-based analysis, where various detection or sequencing method could be employed. It is critically important to study the protein translocating through various 2D nanopores, which may help design efficient nanopore devices. However, few 2D materials other than graphene have been studied in this context yet. In this work, molecular dynamics (MD) simulations were employed to investigate the feasibility of single-molecule protein sequencing with a MoS₂ nanopore. Both phenylalanine–glycine repeat peptides and a peptide with the sequence taken from the thioredoxin protein were studied in their extended unfolded state, which adsorbed onto the MoS₂ membrane spontaneously. These peptides kept adsorbing onto MoS₂ and permeated unidirectionally through the MoS₂ nanopore, driven by either an electric field or hydrostatic pressure gradient. Their translocation process was stepwise, and the speed sensitively depended on the electric field, hydrostatic pressure, the charge density, or hydrophobicity of the peptides. The stepwise peptide translocation yielded ionic current blockades correlating with the sequence of peptide fragment in the nanopore. This work provides with insights for designing a protein-sequencing device with a MoS₂ nanopore

“Jacketing” Effect Liquid Crystalline Polymer with Perylenediimide as Side Chain: Synthesis, Liquid Crystalline Phase, and Photovoltaic Performances

All polymer solar cells (all-PSCs) is one of the important emerging renewable energy technologies. In this work, we use “jacketing” effect liquid crystalline polymer (LCP) with perylenediimide as side chain to fabricate all-PSCs. First, poly­(2,5-bis­{[6-(4-alkoxy-4′-perylenediimide)-6-hexyl]­oxycarbonyl}­styrene) (abbreviated as PPDCS) is successfully synthesized via chain polymerization. The resultant polymer PPDCS forms stable smectic C (SmC) structure until decomposition. The electrochemical experiment indicates PPDCS shows deep LUMO energy level of −3.81 eV, thus, the nonconjugated PPDCS can be employed as acceptor materials to build all-PSCs. Atomic force microscopy (AFM) experiments show that the PBT7/PPDCS blend film forms a bicontinuous network-domains and the resultant film shows extensive absorption spectrum (300–800 nm) on UV–vis spectra. All-PSCs device fabricated by PTB7/PPDCS presents the best power conversion efficiency (PCE) of 1.23% after optimization, where the short-circuit current density (<i>J</i>_sc) is 4.34 mA cm^–2, an open-circuit voltage (<i>V</i>_oc) is 0.65 V, and a fill factor (FF) is 0.37. This work suggests that the nonconjugated LCP shows potential application for solar cell

Discovery of the Highly Selective and Potent STAT3 Inhibitor for Pancreatic Cancer Treatment

Signal transducer and activator of transcription 3 (STAT3) is an attractive cancer therapeutic target. Unfortunately, targeting STAT3 with small molecules has proven to be very challenging, and for full activation of STAT3, the cooperative phosphorylation of both tyrosine 705 (Tyr705) and serine 727 (Ser727) is needed. Further, a selective inhibitor of STAT3 dual phosphorylation has not been developed. Here, we identified a low nanomolar potency and highly selective small-molecule STAT3 inhibitor that simultaneously inhibits both STAT3 Tyr705 and Ser727 phosphorylation. YY002 potently inhibited STAT3-dependent tumor cell growth in vitro and achieved potent suppression of tumor growth and metastasis in vivo. More importantly, YY002 exhibited favorable pharmacokinetics, an acceptable safety profile, and superior antitumor efficacy compared to BBI608 (STAT3 inhibitor that has advanced into phase III trials). For the mechanism, YY002 is selectively bound to the STAT3 Src Homology 2 (SH2) domain over other STAT members, which strongly suppressed STAT3 nuclear and mitochondrial functions in STAT3-dependent cells. Collectively, this study suggests the potential of small-molecule STAT3 inhibitors as possible anticancer therapeutic agents