Revitalizing Skin Repair: Unveiling the Healing Power of Livisin, a Natural Peptide Calcium Mimetic.

When the skin is damaged, accelerating the repair of skin trauma and promoting the recovery of tissue function are crucial considerations in clinical treatment. Previously, we isolated and identified an active peptide (livisin) from the skin secretion of the frog Odorrana livida. Livisin exhibited strong protease inhibitory activity, water solubility, and stability, yet its wound-healing properties have not yet been studied. In this study, we assessed the impact of livisin on wound healing and investigated the underlying mechanism contributing to its effect. Our findings revealed livisin effectively stimulated the migration of keratinocytes, with the underlying mechanisms involved the activation of CaSR as a peptide calcium mimetic. This activation resulted in the stimulation of the CaSR/E-cadherin/EGFR/ERK signaling pathways. Moreover, the therapeutic effects of livisin were partially reduced by blocking the CaSR/E-cadherin/EGFR/ERK signaling pathway. The interaction between livisin and CaSR was further investigated by molecular docking. Additionally, studies using a mouse full-thickness wound model demonstrated livisin could accelerate skin wound healing by promoting re-epithelialization and collagen deposition. In conclusion, our study provides experimental evidence supporting the use of livisin in skin wound healing, highlighting its potential as an effective therapeutic option.

Synthesis and biological evaluation of isatin derivatives containing 1,3,4-thiadiazole as potent a-glucosidase inhibitors.

A series of (Z)-3-(2-(1,3,4-thiadiazol-2-yl)hydrazono)-1-substituted indolin-2-ones derivatives (3a-3m) were designed and synthesized. All newly synthesized compounds were evaluated for their a-glucosidase inhibitory activity with resveratrol as positive control in vitro. Except for 3i and 3j, all of the compounds showed a potent inhibitory activity against a-glucosidase with IC50 values in the range of 3.12 ± 1.25 to 45.95 ± 1.26 µM and the purity of these compounds was greater than 95%. The IC50 values were being compared to the standard resveratrol (IC50 = 22.00 ± 1.15 µM) and it was found that compounds 3b, 3d-3h were found to be more active than resveratrol. Specifically, (Z)-3-(2-(1,3,4-thiadiazol-2-yl)hydrazono)-1-(4-chlorobenzyl)indolin-2-one (3d) exhibited the most potent a-glucosidase inhibitory activity with IC50 value of 3.12 ± 1.25 µM. The kinetic analysis revealed that compound (3d) is noncompetitive inhibitor. Structure activity relationship has been established for all compounds. Furthermore, the binding interactions of compound 3d with the active site of a-glucosidase were confirmed through molecular docking. This study has identified a new class of potent a-glucosidase inhibitors for further investigation.

Biodegradation performance and biofouling control of a halophilic biocarriers-MBR in saline pharmaceutical (ampicillin-containing) wastewater treatment.

This work develops a halophilic biocarriers-MBR for saline pharmaceutical wastewater treatment. The system has effectively treated the ampicillin-containing saline wastewater for 32 days, when the ampicillin concentration is lower than 20 mg/L. The system can tolerate the saline organic wastewater with a reasonable biodegradability (removals of COD over 75%) when the ampicillin concentration is 50 mg/L. The system has a bad performance in biodegradation (COD removals around 60-70%) and fouled within 16 days at a high ampicillin concentration of 100 mg/L. At high transmembrane pressures over 30 KPa, some ampicillin molecules may permeate through the membrane causing decreases in the ampicillin removal. The concentrations of protein and carbohydrate in EPS and SMP have increased over time and with increasing the ampicillin concentration. The method of biofouling control in MBR for the ampicillin situations has been proposed based on monitoring the concentrations of EPS and SMP. The drying-assisted monitoring of membrane biofoulants has showed a better efficiency than the monitoring of transmembrane pressure for membrane anti-biofouling in the treatment of pharmaceutical saline wastewaters where a spectroscopic detection can be hardly applied. This work may benefit relative research works for the control of biodegradation performance and membrane biofouling to better treat saline pharmaceutical wastewaters.

(E)-N'-(4-Hydroxy-benzyl-idene)-2-methoxy-benzohydrazide.

The title compound, C(15)H(14)N(2)O(3), exists in the E configuration with respect to the central methyl-idene unit. The dihedral angle between the two substituted benzene rings is 22.0 (2)°. Within the mol-ecule there is an intra-molecular N-H⋯O hydrogen bond involving the hydro-zide H atom and the O atom of the meth-oxy substituent on the adjacent phenyl ring. In the crystal structure, mol-ecules are linked through inter-molecular O-H⋯O hydrogen bonds, forming zigzag chains along the b direction.

An Immunosensing System Using Stilbene Glycoside as a Fluorogenic Substrate for an Enzymatic Reaction Model.

A natural product, stilbene glycoside (2,3,5,4'-tetrahydroxydiphenylethylene-2-O-glucoside, TBG), has been evaluated for the first time as a potential substrate for horseradish peroxidase (HRP)-catalyzed fluorogenic reactions. The properties of TBG as a fluorogenic substrate for HRP and its application in a fluorometric enzyme-linked immunosensing system were compared with commercially available substrates such as p-hydroxyphenylpropionic acid (pHPPA), chavicol and Amplex red using Brucella melitensis antibody (BrAb) as a model analyte. The immunosensing body based on HRP-BrAb was constructed by dispersing graphite, BrAg and paraffin wax at room temperature. In a competitive immunoassay procedure, the BrAb competed with HRP-BrAb to react with the immobilized BrAg. In the enzymatic reaction, the binding HRP-BrAb on the sensing body surface can catalyze the polymerization reaction of TBG by H2O2 forming fluorescent dimers and causing an increase in fluorescence intensity. TBG showed comparable ability for HRP detection and its enzyme-linked immunosensing reaction system, in a linear detection ranging of 3.5´10-8~7.6´10-6g/L and with a detection limit of 1.7´10-9 g/L. The immobilized biocomposite surface could be regenerated with excellent reproducibility (RSD=3.8%) by simply polishing with an alumina paper. The proposed immunosensing system has been used to determine the BrAb in rabbit serum samples with satisfactory results.