The efficacy and safety of acupoint catgut embedding for peripheral facial paralysis sequela: A protocol for systematic review and meta-analysis.

BACKGROUND: Peripheral facial paralysis sequela (PFPS) is a group of sequence syndrome after the acute onset of peripheral facial paralysis. Nearly 70% of patients with peripheral facial paralysis recover completely, but nearly 30% of patients leave multiple sequelae, which have serious negative impacts on the physical and psychological health of patients. Without a high risk of side effect, acupoint catgut embedding (ACE), a common acupuncture therapy, is widely used to treat this disorder. And a number of studies have shown the efficacy of this therapy for PFPS. But in fact, the evidence of the overall effect of ACE in the treatment of PFPS is still insufficient. Therefore, the purpose of this study is to evaluate the efficiency and safety of ACE for PFPS. METHODS: Two reviewers will collect randomized controlled trials (RCTs) on ACE for PFPS by searching the following databases, including The Cochrane Library, PubMed, Web of Science, EMBASE, China Biomedical Literature (CBM), China National Knowledge Infrastructure (CNKI), Chinese Scientific Journals Database (VIP), and Wanfang database, from their initiation to May 2021. The searching of publications will include English and Chinese without any restriction of countries and regions. Besides, 2 reviewers will independently include in studies that meet the inclusion criteria and extract data we need, then use Cochrane Collaboration's Risk of Bias Tool to assess their methodological quality. The efficacy and safety of ACE as a treatment for PFPS will be assessed according to the synthetic risk ratio (RR), odds ratio (OR), or weighted mean difference (WMD), standardized mean difference (SMD) with consistent 95% confidence intervals (95% CI). And the Review Manager 5.3 software will be adopted to conduct the statistical analysis. RESULTS: The protocol for meta-analysis will systematically evaluate the efficacy and safety of ACE for PFPS. And the final result of this search will provide sufficient evidence and an authentic assessment focusing on the problem. CONCLUSION: This search will explore whether ACE could be used as an effective and non-drug external therapy of TCM for PFPS and offer supports for clinical practice. PROSPERO REGISTRATION NUMBER: CRD42021240004.

Insights into maize starch degradation by high pressure homogenization treatment from molecular structure aspect.

High-pressure homogenization (HPH) is a common physical method used for starch modification. In this study, starch molecular structure in terms of chain-length distribution (CLD) and molecular size is characterized to explore the structural variations during HPH and its internal relations. It is found that: 1) the molecular size is significantly reduced by HPH treatments and further gradually decreases with HPH pressure increasing; 2) HPH degrades the long amylose chains with degree of polymerization (DP) ~ 2000-20,000 into short- and intermediate-amylose chains with DP ~ 100-1000 and DP ~ 1000-2000; 3) by HPH treatment, the proportion of amylopectin chains with DP ~ 6-12 and DP ~ 12-24 decreases while that with DP ~ 24-36 and DP ~ 36-100 increases, whereas, the amylopectin CLDs between HPH treated starch samples are not significantly varied; and 4) by a subtraction analysis, the molecular size of HPH treated starches shows a strong correlation with the proportion of degraded long amylose chains, indicating these long amylose chains might play a critical role in maintaining the large molecular size of starch. This study provides a further understanding of molecular features from the individual chains assembling into a whole branched molecule.

Effect of dry heating treatment on multi-levels of structure and physicochemical properties of maize starch: A thermodynamic study.

Dry heating treatment (DHT) is a common process widely used in food industry. In this study, the thermodynamic effects of DHT on starch structure and physicochemical properties are investigated. The results show that, with heating temperature increasing during DHT, the molecular size, long-amylose chains with degree of polymerization (DP) ~5000-20,000, and the crystallinity of maize starch are significantly reduced while the granular structure is retained with slightly aggregation between starch particles. The solubility of DHT starch increases from 0.5% to 2%, indicating the majority of DHT starch is still insoluble. DHT affects starch thermal property greatly that, it decreases the gelatinization enthalpy while increases the heterogeneity of starch crystallites. With heating temperature increasing, DHT reduces the overall viscosity of starch paste. The rheological property of DHT starch is frequency-dependent, showing the typical shear thinning behavior and "solid-like" gel property. Especially, as heating temperature reaches 190 °C, the shear resistance becomes stronger, and it is closer to Newtonian fluid. The results prove the thermodynamic effects of DHT on multi-levels of starch structure and physicochemical properties, also indicating the great potential to utilize DHT in modifying starch properties and amplifying its applications.

Screening for Novel Small-Molecule Inhibitors Targeting the Assembly of Influenza Virus Polymerase Complex by a Bimolecular Luminescence Complementation-Based Reporter System.

Influenza virus RNA-dependent RNA polymerase consists of three viral protein subunits: PA, PB1, and PB2. Protein-protein interactions (PPIs) of these subunits play pivotal roles in assembling the functional polymerase complex, which is essential for the replication and transcription of influenza virus RNA. Here we developed a highly specific and robust bimolecular luminescence complementation (BiLC) reporter system to facilitate the investigation of influenza virus polymerase complex formation. Furthermore, by combining computational modeling and the BiLC reporter assay, we identified several novel small-molecule compounds that selectively inhibited PB1-PB2 interaction. Function of one such lead compound was confirmed by its activity in suppressing influenza virus replication. In addition, our studies also revealed that PA plays a critical role in enhancing interactions between PB1 and PB2, which could be important in targeting sites for anti-influenza intervention. Collectively, these findings not only aid the development of novel inhibitors targeting the formation of influenza virus polymerase complex but also present a new tool to investigate the exquisite mechanism of PPIs. IMPORTANCE Formation of the functional influenza virus polymerase involves complex protein-protein interactions (PPIs) of PA, PB1, and PB2 subunits. In this work, we developed a novel BiLC assay system which is sensitive and specific to quantify both strong and weak PPIs between influenza virus polymerase subunits. More importantly, by combining in silico modeling and our BiLC assay, we identified a small molecule that can suppress influenza virus replication by disrupting the polymerase assembly. Thus, we developed an innovative method to investigate PPIs of multisubunit complexes effectively and to identify new molecules inhibiting influenza virus polymerase assembly.