PSX804827_supplemental_material – Supplemental material for Land Taking and Electoral Rule Setting: Evidence from Chinese Rural Democracy

Supplemental material, PSX804827_supplemental_material for Land Taking and Electoral Rule Setting: Evidence from Chinese Rural Democracy by Fubing Su, Xi Lu, Xi Zhao and Ran Tao in Political Studies</p

Metal–Organic Framework-Membranized Bicomponent Core–Shell Catalyst HZSM-5@UIO-66-NH₂/Pd for CO₂ Selective Conversion

In this study, a Zr-based metal–organic framework (MOF)-membranized bicomponent core–shell catalyst HZSM-5@UIO-66-NH2/Pd was produced. Monodispersed HZSM-5 zeolites acted as the core for the epitaxial growth of the UIO-66-NH2 shell to obtain MOF membrane coated HZSM-5@UIO-66-NH2 nanocrystals, and Pd nanoparticles were well-dispersed on its membrane surface. The catalyst HZSM-5@UIO-66-NH2/Pd exhibited high CO selectivity (92.2%) in CO2 hydrogenation

New Insight into the Photoprotection Mechanism of Plant Sunscreens: Adiabatic Relaxation Competing with Nonadiabatic Relaxation in the <i>cis</i> → <i>trans</i> Photoisomerization of Methyl Sinapate

A great deal of thermally instable cis form photoisomerization products will be formed from the thermally stable trans form of the plant sunscreens sinapate esters upon ultraviolet radiation. To reveal the photoisomerization mechanism of the cis-isomer, we explore the photodynamics of a model plant sunscreen methyl sinapate (MS) in the cis form in organic solution. The high photoisomerization quantum yield of the cis-isomer results in the relatively higher photostability of trans-MS. By utilizing femtosecond transient absorption spectroscopy and quantum chemical calculation, we propose that an adiabatic relaxation competes with nonadiabatic relaxation for the excited-state cis form of methyl sinapate. These results suggest that the photoprotection mechanism of the cis form of sinapate esters is significantly different from that of the trans form of sinapate esters and plays an important role in the overall photoprotection effect

Heterogeneous nuclear ribonucleoprotein U-actin complex derived from extracellular vesicles facilitates proliferation and migration of human coronary artery endothelial cells by promoting RNA polymerase II transcription

Coronary artery disease (CAD) represents a fatal public threat. The involvement of extracellular vesicles (EVs) in CAD has been documented. This study explored the regulation of embryonic stem cells (ESCs)-derived EVs-hnRNPU-actin complex in human coronary artery endothelial cell (HCAEC) growth. Firstly, in vitro HCAEC hypoxia models were established. EVs were extracted from ESCs by ultracentrifugation. HCAECs were treated with EVs and si-VEGF for 24 h under hypoxia, followed by assessment of cell proliferation, apoptosis, migration, and tube formation. Uptake of EVs by HCAECs was testified. Additionally, hnRNPU, VEGF, and RNA Pol II levels were determined using Western blotting and CHIP assays. Interaction between hnRNPU and actin was evaluated by Co-immunoprecipitation assay. HCAEC viability and proliferation were lowered, apoptosis was enhanced, wound fusion was decreased, and the number of tubular capillary structures was reduced under hypoxia, whereas ESC-EVs treatment counteracted these effects. Moreover, EVs transferred hnRNPU into HCAECs. EVs-hnRNPU-actin complex increased RNA Pol II level on the VEGF gene promoter and promoted VEGF expression in HCAECs. Inhibition of hnRNPU or VEGF both annulled the promotion of EVs on HCAEC growth. Collectively, ESC-EVs-hnRNPU-actin increased RNA Pol II phosphorylation and VEGF expression, thus promoting HCAEC growth.</p

Insight into the impact of environments on structure of chimera C3 of human β-defensins 2 and 3 from molecular dynamics simulations

<div><p>C3 is a chimera from human β-defensins 2 and 3 and possesses higher antimicrobial activity compared with its parental molecules, so it is an attractive candidate for clinical application of antimicrobial peptides. In continuation with the previous studies, molecular dynamics (MD) simulations were carried out for further investigating the effect of ambient environments (temperature and bacterial membrane) on C3 dynamics. Our results reveal that C3 has higher flexibility, larger intensity of motion, and more relevant secondary structural changes at 363 K to adapt the high temperature and maintain its antimicrobial activity, comparison with it at 293 K; when C3 molecule associates with the bacterial membrane, it slightly fluctuates and undergoes local conformational changes; in summary, C3 molecule demonstrates stable conformations under these environments. Furthermore, MD results analysis show that the hydrophobic contacts, the hydrogen bonds, and disulfide bonds in the peptide are responsible for maintaining its stable conformation. In addition, our simulation shows that C3 peptides can make anionic lipids clustered in the bacterial membrane; it means that positive charges and pronounced regional cationic charge density of C3 are most key factors for its antimicrobial activity.</p></div

Inhibition mechanism understanding from molecular dynamics simulation of the interactions between several flavonoids and proton-dependent glucose transporter

Proton-dependent glucose transporters as important drug targets can have different protonation states and adjust their conformational state under different pHs. So based on this character, research on its inhibition mechanism is a significant work. In this article, to study its inhibitory mechanism, we performed the molecular dynamics of several classical flavonoid molecules (Three inhibitors Phloretin, Naringenin, Resveratrol. Two non-inhibitors Isoliquiritigenin, Butein) with glucose transporters under two distinct environmental pHs. The results show inhibitors occupy glucose binding sites (GLN137, ILE255, ASN256) and have strong hydrophobic interactions with proteins through core moiety (C6-Cn-C6). In addition, inhibitors had better inhibitory effects in protonation state. In contrast, non-inhibitors can not occupy glucose binding sites (GLN137, ILE255, ASN256), thus they do not have intense interactions with the protein. It is suggested that favorable inhibitors should effectively take up the glucose-binding site (GLN137, ILE255, ASN256) and limit the protein conformational changes. Communicated by Ramaswamy H. Sarma</p