Composting is an efficient way to convert organic waste into fertilizers. However, waste materials often contain large amounts of antibiotic resistance genes (ARGs) and mobile genetic elements (MGEs) that can reduce the efficacy of antibiotic treatments when transmitted to humans. Because conventional composting often fails to remove these compounds, we evaluated if hyperthermophilic composting with elevated temperature is more efficient at removing ARGs and MGEs and explored the underlying mechanisms of ARG removal of the two composting methods. We found that hyperthermophilic composting removed ARGs and MGEs more efficiently than conventional composting (89% and 49%, respectively). Furthermore, the half-lives of ARGs and MGEs were lower in hyperthermophilic compositing compared to conventional composting (67% and 58%, respectively). More-efficient removal of ARGs and MGEs was associated with a higher reduction in bacterial abundance and diversity of potential ARG hosts. Partial least-squares path modeling suggested that reduction of MGEs played a key role in ARG removal in hyperthermophilic composting, while ARG reduction was mainly driven by changes in bacterial community composition under conventional composting. Together these results suggest that hyperthermophilic composting can significantly enhance the removal of ARGs and MGEs and that the mechanisms of ARG and MGE removal can depend on composting temperature.

Despite the availability of effective drugs, blood pressure (BP) control remains poor among most populations. To explore the effects of interactive mobile health (mhealth) intervention on BP management and find out the optimal target population, we performed a systematic review and meta-analysis of randomized controlled trials to estimate the pooled effects of mhealth intervention on BP control. PubMed, EMBASE, Cochrane Library, and CNKI were searched to identify eligible randomized controlled trials published between January 15, 2007 and April 28, 2019, and bibliographies of eligible articles were further reviewed. Random-effect models were utilized to pool estimates of net changes in systolic BP and diastolic BP between mhealth intervention group and control group. Eleven randomized controlled trials met the inclusion criteria, with a total sample size of 4271 participants. Compared with the control group, mhealth intervention was associated with significant changes in systolic BP and diastolic BP of −3.85 mm Hg; 95% CI, −4.74 to −2.96 and −2.19 mm Hg; 95% CI, −3.16 to −1.23, respectively. Subgroup analyses revealed consistent effects across study duration and intervention intensity subgroups. In addition, participants with inadequate BP control at recruitment might gain more benefits with mhealth intervention. Therefore, interactive mhealth intervention may be a useful tool for improving BP control among adults, especially among those with inadequate BP control.

No abstract

Effects of hydrophobic and electrostatic interactions on the self-assembling process of the ionic-complementary peptide EMK16-II are investigated by atomic force microscopy imaging, circular dichroism spectra, light scattering, and chromatography. It is found that the hydrophobicity of the peptide promotes the aggregation in pure water even at a very low concentration, resulting in a much lower critical aggregation concentration than that of another peptide, EAK16-II. The effect of anions in solution with different valences on electrostatic interactions is also important. Monovalent anions (Cl(-) and Ac(-)) with a proper concentration can facilitate the formation of peptide fibrils, with Cl(-) of smaller size being more effective than Ac(-) of larger size. However, only small amounts of fibrils, but plenty of large amorphous aggregates, are found when the peptide solution is incubated with multivalent anions, such as SO(4)(2-), C(6)H(5)O(7) (3-), and HPO(4)(2-). More importantly, by gel filtration chromatography, the citrate anion, which induces a similar effect on the self-assembling process of EMK16-II as that of SO(4)(2-) and HPO(4)(2-), can interact with two or more positively charged residues of the peptide and reside in the amorphous aggregates. This implies a "salt bridge" effect of multivalent anions on the peptide self-assembling process, which can interpret a previous puzzle why divalent cations inhibit the formation of ordered nanofibrils of the ionic-complementary peptides. Thus, our results clarify the important effects of hydrophobic and electrostatic interactions on the self-assembling process of the ionic-complementary peptides. These are greatly helpful for us to understand the mechanism of peptides' self-assembling process and protein folding and aggregation.