Egg white hydrolysate peptides act as antimicrobial and anti-inflammatory agents for acne.

A simple method to generate antibacterial peptides by alkaline hydrolysis of hen egg whites is reported. The method reproducibly generates short peptides with molecular weight of less than 14.4 kDa that exhibit low to no cytotoxicity on RAW 264.7 macrophage cells, but do inhibit the bacterial growth of Cutibacterium acnes (C. acnes), Staphylococcus aureus (S. aureus) and antibiotic-resistant S. aureus (MRSA), while also reducing nitric oxide production from heat-killed C. acnes-treated RAW 264.7 cells. Peptidomics revealed at least thirty peptides within the complex mixture, of which eight were evaluated individually. Three peptides (PK8, EE9 and RP8) were potent anti-inflammation and antibacterial agents, but notably the complex egg white hydrolysate (EWH) was more effective than the individual peptides. Electron microscopy suggests the antibacterial mechanism of both the hydrolysate and the selected peptides is through disruption of the cell membrane of C. acnes. These findings suggest that EWH and EWH-derived peptides are promising candidates for infection and inflammation treatment, particularly in managing acne and combating antibiotic-resistant bacteria like MRSA.

A New Source and Large Quantity of Resveratrol in Cratoxylum Species and Their Activities on Normal Human and Cancer Cells.

Cratoxylum formosum ssp. formosum (Cff), C. formosum ssp. pruniflorum (Cfp), and C. sumatranum (Cs) were investigated for phytochemical analysis. Toxicity testing, programmed cell death, and cell cycle arrest were tested on CHL-1, HCT-116, and HepG2 cancer cell lines, and human normal PBMCs. The results are revealed in the following order. The phytochemical percentages varied in each species, the quantity and concentration of α-amyrin and resveratrol were 0.038 mg/g and 0.955 mg/mL, and 0.064 mg/g and 0.640 mg/mL. The most studied Cratoxylum extracts showed IC50 values in PBMCs and cancer cell lines except for the hexane Cff and ethanol Cfp extracts. All studied extracts did not induce DNA breaks in PBMCs but caused significant DNA breaks in the cancer cell lines. All studied extracts induced both apoptosis and necrosis in cancer cell lines, and the DNA quantity in the S and G2-M phases decreased significantly but did not induce apoptosis and necrosis in PBMCs. Except for the ethanolic extracts of Cff and Cfp that induced PBMCs apoptosis and necrosis, these data confirmed that the three studied Cratoxylum samples have inhibiting properties for the growth of cancer cells and low toxicity to PBMCs. Cs showed more toxicity to cancer cell lines than Cf and cisplatin.

Development in competitive immunoassay of a point-of-care testing for cotinine (COT) detection in urine.

We present a sensitive and selective lateral flow immunoassay (LFIA) for cotinine (COT), the primary metabolite of nicotine. COT is widely recognized as a superior biomarker to evaluate tobacco smoke exposure. The LFIA uses a competitive assay format where the COT-BSA capture competes with the target COT in urine samples for binding to the monoclonal antibody against COT (mAb-COT) conjugated with gold nanoparticles (mAb-COT-AuNPs). To improve the sensitivity and selectivity of the LFIA-COT, we focused on optimizing the diameter of AuNPs, the conjugation of mAb-COT, and the concentration of the COT-BSA capture. Our findings reveal that the utilization of 40 nm AuNPs in conjugation with a concentration of 4 mg mL-1 of mAb-COT demonstrated significantly greater efficacy compared to LFAs utilizing 20 nm AuNPs. Under the optimal conditions, the LFIA-COT demonstrated sensitive detection of COT at a level of 150 ng mL-1 within 15 min, as observed by the naked eye. It possesses a linear range of 25 to 200 ng mL-1 of COT, with the limit of detection (LOD) of 11.94 ng mL-1 in human urine samples when the color intensity is analyzed using ImageJ software. Our LFIA described here is simple and requires less time for COT detection. It can be used for the rapid and quantitative detection of COT in urine samples in clinical settings.

Structure-based epitope prediction and assessment of cross-reactivity of Myrmecia pilosula venom-specific IgE and recombinant Sol g proteins (Solenopsis geminata).

The global distribution of tropical fire ants (Solenopsis geminata) raises concerns about anaphylaxis and serious medical issues in numerous countries. This investigation focused on the cross-reactivity of allergen-specific IgE antibodies between S. geminata and Myrmecia pilosula (Jack Jumper ant) venom proteins due to the potential emergence of cross-reactive allergies in the future. Antibody epitope analysis unveiled one predominant conformational epitope on Sol g 1.1 (PI score of 0.989), followed by Sol g 2.2, Sol g 4.1, and Sol g 3.1. Additionally, Pilosulin 1 showed high allergenic potential (PI score of 0.94), with Pilosulin 5a (PI score of 0.797) leading in B-cell epitopes. The sequence analysis indicated that Sol g 2.2 and Sol g 4.1 pose a high risk of cross-reactivity with Pilosulins 4.1a and 5a. Furthermore, the cross-reactivity of recombinant Sol g proteins with M. pilosula-specific IgE antibodies from 41 patients revealed high cross-reactivity for r-Sol g 3.1 (58.53%) and r-Sol g 4.1 (43.90%), followed by r-Sol g 2.2 (26.82%), and r-Sol g 1.1 (9.75%). Therefore, this study demonstrates cross-reactivity (85.36%) between S. geminata and M. pilosula, highlighting the allergenic risk. Understanding these reactions is vital for the prevention of severe allergic reactions, especially in individuals with pre-existing Jumper Jack ant allergy, informing future management strategies.

Protein-Ligand Binding and Structural Modelling Studies of Pheromone-Binding Protein-like Sol g 2.1 from Solenopsis geminata Fire Ant Venom.

Sol g 2 is the major protein in Solenopsis geminata fire ant venom. It shares the highest sequence identity with Sol i 2 (S. invicta) and shares high structural homology with LmaPBP (pheromone-binding protein (PBP) from the cockroach Leucophaea maderae). We examined the specific Sol g 2 protein ligands from fire ant venom. The results revealed that the protein naturally formed complexes with hydrocarbons, including decane, undecane, dodecane, and tridecane, in aqueous venom solutions. Decane showed the highest affinity binding (Kd) with the recombinant Sol g 2.1 protein (rSol g 2.1). Surprisingly, the mixture of alkanes exhibited a higher binding affinity with the rSol g 2.1 protein compared to a single one, which is related to molecular docking simulations, revealing allosteric binding sites in the Sol g 2.1 protein model. In the trail-following bioassay, we observed that a mixture of the protein sol g 2.1 and hydrocarbons elicited S. geminata worker ants to follow trails for a longer time and distance compared to a mixture containing only hydrocarbons. This suggests that Sol g 2.1 protein may delay the evaporation of the hydrocarbons. Interestingly, the piperidine alkaloids extracted have the highest attraction to the ants. Therefore, the mixture of hydrocarbons and piperidines had a synergistic effect on the trail-following of ants when both were added to the protein.

Proteomic analysis of crocodile white blood cells reveals insights into the mechanism of the innate immune system.

Crocodiles have a particularly powerful innate immune system because their blood contains high levels of antimicrobial peptides. They can survive injuries that would be fatal to other animals, and they are rarely afflicted with diseases. To better understand the crocodile's innate immune response, proteomic analysis was performed on the white blood cells (WBC) of an Aeromonas hydrophila-infected crocodile. Levels of WBC and red blood cells (RBC) rapidly increased within 1 h. In WBC, there were 109 up-regulated differentially expressed proteins (DEP) that were up-regulated. Fifty-nine DEPs dramatically increased expression from 1 h after inoculation, whereas 50 up-regulated DEPs rose after 24 h. The most abundant DEPs mainly had two biological functions, 1) gene expression regulators, for example, zinc finger proteins and histone H1 family, and 2) cell mechanical forces such as actin cytoskeleton proteins and microtubule-binding proteins. This finding illustrates the characteristic effective innate immune response mechanism of crocodiles that might occur via boosted transcription machinery proteins to accelerate cytoskeletal protein production for induction of phagocytosis, along with the increment of trafficking proteins to transport essential molecules for combating pathogens. The findings of this study provide new insights into the mechanisms of the crocodile's innate immune system.

Rational design of an N-terminal cysteine-containing tetrapeptide that inhibits tyrosinase and evaluation of its mechanism of action.

There has been a resurgence of interest in bioactive peptides as therapeutic agents. This is particularly interesting for tyrosinase, which can be inhibited by thiol-containing peptides. This work demonstrates that an N-terminal cysteine-containing tetrapeptide can be rationally designed to inhibit tyrosinase activity in vitro and in cells. The tetrapeptide cysteine (C), arginine (R), asparagine (N) and leucine (L) or CRNL is a potent inhibitor of tyrosinase activity with an IC50 value of 39.62 ± 6.21 µM, which is comparable to currently used tyrosinase inhibitors. Through structure-activity studies and computational modeling, we demonstrate the peptide interacts with the enzyme via electrostatic (R with E322), hydrogen bonding (N with N260) and hydrophobic (L with V248) intermolecular interactions and that a combination of these is required for potent activity. Moreover, copper chelating activity might be one of the mechanisms of tyrosinase inhibition by CRNL. Kinetic studies show that tetrapeptide is a competitive inhibitor with two-step irreversible inhibition. In addition, CRNL had no toxicity and could reduce melanin levels in the murine melanoma cell line (B16F1). Overall, CRNL is a very promising candidate for hyperpigmentation treatment.

Characterization and Localization of Sol g 2.1 Protein from Solenopsis geminata Fire Ant Venom in the Central Nervous System of Injected Crickets (Acheta domestica).

Solenopsis geminata is recognized for containing the allergenic proteins Sol g 1, 2, 3, and 4 in its venom. Remarkably, Sol g 2.1 exhibits hydrophobic binding and has a high sequence identity (83.05%) with Sol i 2 from S. invicta. Notably, Sol g 2.1 acts as a mediator, causing paralysis in crickets. Given its structural resemblance and biological function, Sol g 2.1 may play a key role in transporting hydrophobic potent compounds, which induce paralysis by releasing the compounds through the insect's nervous system. To investigate this further, we constructed and characterized the recombinant Sol g 2.1 protein (rSol g 2.1), identified with LC-MS/MS. Circular dichroism spectroscopy was performed to reveal the structural features of the rSol g 2.1 protein. Furthermore, after treating crickets with S. geminata venom, immunofluorescence and immunoblotting results revealed that the Sol g 2.1 protein primarily localizes to the neuronal cell membrane of the brain and thoracic ganglia, with distribution areas related to octopaminergic neuron cell patterns. Based on protein-protein interaction predictions, we found that the Sol g 2.1 protein can interact with octopamine receptors (OctRs) in neuronal cell membranes, potentially mediating Sol g 2.1's localization within cricket central nervous systems. Here, we suggest that Sol g 2.1 may enhance paralysis in crickets by acting as carriers of active molecules and releasing them onto target cells through pH gradients. Future research should explore the binding properties of Sol g 2.1 with ligands, considering its potential as a transporter for active molecules targeting pest nervous systems, offering innovative pest control prospects.

Rational design and characterization of cell-selective antimicrobial peptides based on a bioactive peptide from Crocodylus siamensis hemoglobin.

Antimicrobial resistance is a growing health concern. Antimicrobial peptides are a potential solution because they bypass conventional drug resistance mechanisms. Previously, we isolated a peptide from Crocodylus siamensis hemoglobin hydrolysate, which has antimicrobial activity and identified the main peptide from this mixture (QL17). The objective of this work was to evaluate and rationally modify QL17 in order to: (1) control its mechanism of action through bacterial membrane disruption; (2) improve its antimicrobial activity; and (3) ensure it has low cytotoxicity against normal eukaryotic cells. QL17 was rationally designed using physicochemical and template-based methods. These new peptide variants were assessed for: (1) their in vitro inhibition of microbial growth, (2) their cytotoxicity against normal cells, (3) their selectivity for microbes, and (4) the mode of action against bacteria using scanning electron microscopy (SEM), transmission electron microscopy (TEM) and confocal microscopy. The results indicate that all designed peptides have more potent antimicrobial efficacy than QL17 and IL15 peptides. However, only the most rationally modified peptides showed strong antimicrobial activity and minimal toxicity against normal cells. In particular, IL15.3 (hydrophobicity of 47% and net charge of + 6) was a potent antimicrobial agent (MIC = 4-12 µg/mL; MBC = 6-25 µg/mL) and displayed excellent selectivity for microbes (cf. human cells) via FACS assays. Microscopy confirmed that IL15.3 acts against bacteria by disrupting the cell membrane integrity and penetrating into the membrane. This causes the release of intracellular content into the outer environment leading to the death of bacteria. Moreover, IL15.3 can also interact with DNA suggesting it could have dual mode of action. Overall, a novel variant of QL17 is described that increases antimicrobial activity by over 1000-fold (~ 5 µg/mL MIC) and has minimal cytotoxicity. It may have applications in clinical use to treat and safeguard against bacteria.

The effect of edible bird's nests on the expression of MHC-II and costimulatory molecules of C57BL/6 mouse splenocytes.

The glutinous nest that builds by the saliva secretion of swiftlet is recognizable as an edible bird's nest (EBN). It enriched a medicinal value and was regarded as supplementary food that exerts various beneficial health effects, especially immune boosters. This study's objective was to determine the impact of EBN on the expression of MHC-II and costimulatory molecules (CD86 and CD80) related to the initiation of T-cell activation. Both rEBN and pEBN samples were prepared with simulated gastrointestinal digestion for enhancing the bioaccessibility of bioactive compounds. Our result showed that digested EBN samples slightly influence the upregulation of MHC-II, CD86, and CD80 in gene expression of LPS-stimulated Raw 264.7 cells. The concern of endotoxin contamination in EBN samples, which may cause a false-positive result, was measured by quantitative PCR. We found that the inflammatory genes (IL-1ß and TNF-α) were not induced by EBN treatments. Moreover, cell surface protein expression in splenocytes treated with EBN was assessed using flow cytometric analysis. Digested EBN samples demonstrated their capacity to promote the elevation of MHC-II, CD86, and CD80 cell surface protein expression. Finally, the digested-EBN-treated splenocytes only exhibited a specific response in the T-cells population. Thus, EBN is a source of the bioactive compound that has been proposed to exert a role in the stimulation of both MHC-II and costimulatory molecules for TCR/pMHC-II interaction leading to T-cell activation.

Computational model for lipid binding regions in phospholipase (Ves a 1) from Vespa venom.

The Thai banded tiger wasp (Vespa affinis) is a dangerous vespid species found in Southeast Asia, and its stings often result in fatalities due to the presence of lethal phospholipase A[Formula: see text], known as Vespapase or Ves a 1. Developing anti-venoms for Ves a 1 using chemical drugs, such as chemical drug guide, remains a challenging task. In this study, we screened 2056 drugs against the opening conformation of the venom using the ZINC 15 and e-Drug 3D databases. The binding free energy of the top five drug candidates complexed with Ves a 1 was calculated using 300-ns-MD trajectories. Our results revealed that voxilaprevir had a higher binding free energy at the catalytic sites than other drug candidates. Furthermore, the MD simulation results indicated that voxilaprevir formed stable conformations within the catalytic pocket. Consequently, voxilaprevir could act as a potent inhibitor, opening up avenues for the development of more effective anti-venom therapeutics for Ves a 1.

Electrochemical biosensor based on cellulose nanofibers/graphene oxide and acetylcholinesterase for the detection of chlorpyrifos pesticide in water and fruit juice.

In this work, cellulose nanofibers and graphene oxide are used to fabricate a simple and reliable electrochemical biosensor, based on acetylcholinesterase (AChE) for the detection of highly dangerous organophosphates (OPs), utilizing chlorpyrifos as a representative sample. AChE is an enzyme that is essential for neurotransmission and catalyzes the conversion of acetylcholine (ATCh) into thiocholine and acetic acid. The pesticide used in this work, chlorpyrifos, inhibits the catalytic activity of AChE on ATCh, and this inhibition can be measured using square wave voltammetry (SWV). Utilizing a process of surface modification, layers of cellulose nanofibers, graphene oxide, a chitosan-graphene oxide composite, and acetylcholinesterase (AChE/CS-GO/GO/CNFs) were immobilized on a screen-printed carbon electrode (SPCE). The modified SPCE working electrode was characterized using scanning electron microscopy and graphene oxide trapped in the cellulose nanofibers was found to increase the sensitivity of the biosensor. The modified biosensor demonstrated good performance for detection of chlorpyrifos over a linear range of 25-1000 nM under optimum conditions, and the limits of detection and quantification were 2.2 nM and 73 nM, respectively. Our sophisticated technique might offer a more precise, straightforward, quick, and environmentally friendly way to assess chlorpyrifos contamination in water and juice samples.

Rational Design of RN15m4 Cathelin Domain-Based Peptides from Siamese Crocodile Cathelicidin Improves Antimicrobial Activity.

Antimicrobial peptides are becoming a new generation of antibiotics due to their therapeutic potential and ability to decrease drug-resistant bacteria development. Cathelicidins are known as effective peptides of vertebrate immunity that play crucial roles in the defensive strategy against pathogens. To improve its potency, the RN15 antibacterial peptide derived from the cathelin domain of Crocodylus siamensis cathelicidin has been modified and its antimicrobial properties investigated. Peptides were derived by template-based and physicochemical designation. The RN15 derivative peptides were predicted through their structure modeling, antimicrobial potency, and peptide-membrane calculation. The antimicrobial and cytotoxic activities of candidate peptides were investigated. Simultaneous consideration of physicochemical characteristics, secondary structure modeling, and the result of antimicrobial peptide tools prediction indicated that RN15m4 peptide was a candidate derivative antimicrobial peptide. The RN15m4 peptide expresses antimicrobial activity against most Gram-positive and Gram-negative bacteria and fungi with a lower minimum inhibition concentration (MIC) than the parent peptide. Besides, the time-killing assay shows that the designed peptide performed its ability to quickly kill bacteria better than the original peptide. Scanning electron microscopy (SEM) displayed the destruction of the bacterial cell membrane caused by the RN15m4 peptide. In addition, the RN15m4 peptide exhibits low hemolytic activity and low cytotoxic activity as good as the template peptide. The RN15m4 peptide performs a range of antimicrobial activities with low cell toxicity. Our study has illustrated the combination approach to peptide design for potent antibiotic peptide discovery.

Unveiling the Potent Antiviral and Antioxidant Activities of an Aqueous Extract from Caesalpinia mimosoides Lamk: Cheminformatics and Molecular Docking Approaches.

Our group previously demonstrated that Caesalpinia mimosoides Lamk exhibits many profound biological properties, including anticancer, antibacterial, and antioxidant activities. However, its antiviral activity has not yet been investigated. Here, the aqueous extract of C. mimosoides was prepared from the aerial parts (leaves, stalks, and trunks) to see whether it exerts anti-influenza (H1N1) effects and to reduce the organic solvents consumed during extraction, making it a desirable approach for the large-scale production for medical uses. Our plant extract was quantified to contain 7 g of gallic acid (GA) per 100 g of a dry sample, as determined using HPLC analysis. It also exerts potent antioxidant activities comparable to those of authentic GA. According to untargeted metabolomics (UPLC-ESI(-)-QTOF-MS/MS) with the aid of cheminformatics tools (MetFrag (version 2.1), SIRIUS (version 5.8.3), CSI:FingerID (version 4.8), and CANOPUS), the major metabolite was best annotated as "gallic acid", phenolics (e.g., quinic acid, shikimic acid, and protocatechuic acid), sugar derivatives, and dicarboxylic acids were deduced from this plant species for the first time. The aqueous plant extract efficiently inhibited an influenza A (H1N1) virus infection of MDCK cells with an IC50 of 5.14 µg/mL. Of equal importance, hemolytic activity was absent for this plant extract, signifying its applicability as a safe antiviral agent. Molecular docking suggested that GA interacts with conserved residues (e.g., Arg152 and Asp151) located in the catalytic inner shell of the viral neuraminidase (NA), sharing the same pocket as those of anti-neuraminidase drugs, such as laninamivir and oseltamivir. Additionally, other metabolites were also found to potentially interact with the active site and the hydrophobic 430-cavity of the viral surface protein, suggesting a possibly synergistic effect of various phytochemicals. Therefore, the C. mimosoides aqueous extract may be a good candidate for coping with increasing influenza virus resistance to existing antivirals.

Polydopamine Nanoparticles Functionalized Electrochemical DNA Aptasensor for Serum Glycated Albumin Detection.

Polydopamine (PDA) has now been widely applied to electrochemical biosensing because of its excellent biocompatibility, abundant functional groups, and facile preparation. In this study, polydopamine nanoparticles (PDA-NPs)-functionalized electrochemical aptasensor was developed for the rapid, sensitive, and cost-effective detection of glycated albumin (GA), a promising biomarker for glycemic control in diabetic patients. PDA-NPs were synthesized at various pH conditions in Tris buffer. Cyclic voltammetry (CV) of PDA-NPs-coated screen-printed carbon electrodes (SPCEs) revealed that the materials were more conductive when PDA-NPs were synthesized at pH 9.5 and 10.5 than that at pH 8.5. At pH 10.5, the prepared PDA and PDA-aptamer NPs were monodispersed spherical morphology with an average size of 118.0 ± 1.9 and 127.8 ± 2.0 nm, respectively. When CV and electrochemical impedance spectrometry (EIS) were used for the characterization and detection of the electrochemical aptasensor under optimal conditions, the proposed aptasensor exhibited a broad linearity for detection of GA at a clinically relevant range of (1-10,000 µg mL-1), provided a low detection limit of 0.40 µg mL-1, appreciable reproducibility (less than 10%), and practicality (recoveries 90-104%). In addition, our developed aptasensor presented a great selectivity towards GA, compared to interfering substances commonly present in human serum, such as human serum albumin, urea, glucose, and bilirubin. Furthermore, the evaluation of the aptasensor performance against GA-spiked serum samples showed its probable applicability for clinical use. The developed PDA aptasensor demonstrated excellent sensitivity and selectivity towards GA detection with a simple and facile fabrication process. This proposed technique shows its potential application in GA measurement for improving the screening and management of diabetic patients in the future.

TA-AgNPs/Alginate Hydrogel and Its Potential Application as a Promising Antibiofilm Material against Polymicrobial Wound Biofilms Using a Unique Biofilm Flow Model.

The presence of biofilm within a chronic wound may delay the healing process. Thus, control of biofilm formation and providing bactericidal effect are crucial factors for wound healing management. Alginate-based nanocomposite hydrogels have been suggested as dressing materials for wound treatment, which are employed as a biocompatible matrix. Therefore, in this study, we aimed to develop a biocompatible antimicrobial wound dressing containing AgNPs and demonstrate its efficacy against polymicrobial wound biofilms by using a biofilm flow device to simulate a chronic infected, exuding wound and specific wound environment. The results from agar well diffusion, the Minimum Inhibitory Concentration (MIC) and Minimum Bactericidal Concentration (MBC) assays showed that TA-AgNPs exhibited antibacterial activity against wound pathogens. Additionally, the Minimum Biofilm Eradication Concentration assay (MBEC) demonstrated it could impair biofilm formation. Importantly, our TA-AgNPs/Alginate hydrogel clearly showed antibacterial activities against Streptococcus pyogenes, Staphylococcus aureus and Pseudomonas aeruginosa. Furthermore, we used the biofilm flow device to test the topical antimicrobial hydrogel against a three-species biofilm. We found that TA-AgNPs/Alginate hydrogel significantly showed a 3-4 log reduction in bacterial numbers when applied with multiple doses at 24 h intervals, and was especially effective against the chronic wound pathogen P. aeruginosa. This work highlighted that the TA-AgNPs/Alginate hydrogel is a promising material for treating complex wound biofilms.

Human health risk assessment of PM2.5-bound heavy metal of anthropogenic sources in the Khon Kaen Province of Northeast Thailand.

The study aimed to assess the human health risk of PM2.5-bound heavy metals from anthropogenic sources in Khon Kaen Province, Thailand between December 2020 and February 2021. According to the findings, the geometric mean concentration of PM2.5 in the university area, residential area, industrial zone, and the agricultural zone was 32.78 µg/m3, 50.25 µg/m3, 44.48 µg/m3, and 29.53 µg/m3, respectively. The results showed that the estimated human health risk assessment, in terms of non-carcinogenic risks among children and adults in an urban area (residential and university), industrial zone, and the agricultural area, was of hazard index (HI) value of >1.0 indicating a greater chance of chronic effects occurring. This study showed that exposure to PM2.5-bound heavy metal may increase the likelihood that lasting effects will result in a very high carcinogenic risk (CR) in children in residential areas, and an industrial zone with total carcinogenic risk (TCR) values of 0.23 × 10 1 , and 0.12 × 10 1 , respectively while resulting in a high TCR of 3.34 × 10 - 2 and 4.11 × 10 - 2 within the university areas and agricultural zone, respectively. In addition, health risk assessments among adults demonstrate high TCR values of 4.40 × 10 - 1 (residential area), 2.28 × 10 - 1 (industrial zone), and 7.70 × 10 - 3 (agricultural zone), thus indicating a potential health risk to adults living in these areas while the university area was very low effects on carcinogenic risk ( CR ≤ 10 - 8 ) for adults. Therefore, lowering the risk of exposure to PM2.5 via the respiratory tract, for example, wearing a mask outside is a very effective self-defense strategy for people within and around the study site. This data study strongly supports the implementation of the air pollutant emission source reduction measures control and health surveillance.

In Silico and In Vitro Structure-Activity Relationship of Mastoparan and Its Analogs.

Antimicrobial peptides are an important class of therapeutic agent used against a wide range of pathogens such as Gram-negative and Gram-positive bacteria, fungi, and viruses. Mastoparan (MpVT) is an α-helix and amphipathic tetradecapeptide obtained from Vespa tropica venom. This peptide exhibits antibacterial activity. In this work, we investigate the effect of amino acid substitutions and deletion of the first three C-terminal residues on the structure-activity relationship. In this in silico study, the predicted structure of MpVT and its analog have characteristic features of linear cationic peptides rich in hydrophobic and basic amino acids without disulfide bonds. The secondary structure and the biological activity of six designed analogs are studied. The biological activity assays show that the substitution of phenylalanine (MpVT1) results in a higher antibacterial activity than that of MpVT without increasing toxicity. The analogs with the first three deleted C-terminal residues showed decreased antibacterial and hemolytic activity. The CD (circular dichroism) spectra of these peptides show a high content α-helical conformation in the presence of 40% 2,2,2-trifluoroethanol (TFE). In conclusion, the first three C-terminal deletions reduced the length of the α-helix, explaining the decreased biological activity. MpVTs show that the hemolytic activity of mastoparan is correlated to mean hydrophobicity and mean hydrophobic moment. The position and spatial arrangement of specific hydrophobic residues on the non-polar face of α-helical AMPs may be crucial for the interaction of AMPs with cell membranes.

Novel non-cytotoxic antimicrobial peptides WSKK11 and WSRR11 with potent activity against Cutibacterium acnes.

OBJECTIVES: Cutibacterium acnes is one of the common multifactorial causes that play an important role in the pathophysiology of acne vulgaris. We aimed to develop novel antimicrobial peptides for reduction of the hypercolonization. METHODS: Six cationic peptides were derived by de novo designation. The antimicrobial and cytotoxic activities of peptides were investigated. The peptide conformation was determined by circular dichroism spectrometry. The antimicrobial effects of peptides were evaluated using scanning electron microscopy (SEM), transmission electron microscopy (TEM) and DNA-binding ability assay. RESULTS: Among designed peptides, WSKK11 and WSRR11 were effective antimicrobials against C. acnes at MICs of 128 and 64 mg/L, respectively. The MICs of WSKK11 against Staphylococcus epidermidis, Staphylococcus aureus and Candida albicans were 8, 8 and 32 mg/L, while those of WSRR11 were 64, 32 and 32 mg/L, respectively. WSKK11 and WSRR11 were less toxic to human erythrocytes (<2%) and not toxic to macrophages, keratinocytes and fibroblasts up to 512 mg/L. WSKK11 and WSRR11 mostly revealed the conformation of the undefined or random coil structures under mimicked environmental conditions. The peptides affected cell surfaces and cell membranes of C. acnes as well as possibly translocating through the cell membrane, observed by a combination of SEM and TEM, respectively. WSKK11 and WSRR11 had the ability to bind bacterial DNA. CONCLUSIONS: The two novel antimicrobial peptides WSKK11 and WSRR11 are members of a new class of antimicrobial agents that could deal with acne problems. Therefore, the antimicrobial peptides may be promising novel active agents for dermatological, beauty and cosmeceutical applications.

Anisotropic Silver Nanoparticles Gel Exhibits Antibacterial Action and Reduced Scar Formation on Wounds Contaminated with Methicillin-Resistant Staphylococcus pseudintermedius (MRSP) in a Mice Model.

Staphylococcus pseudintermedius (S. pseudintermedius) infected wounds can cause seriously delayed wound healing processes in animals. Antimicrobial agents that have antimicrobial and wound healing efficacy have become an essential tool for overcoming this problem. In our previous study, anisotropic AgNPs have been reported to have antimicrobial efficiency against animal and human pathogens, and could be suitable as antimicrobial agents for infected wounds. Here, antimicrobial and wound healing activities of anisotropic AgNPs gels were assessed in vivo. BALB/cAJcl mice wounds were infected by Methicillin-resistant Staphylococcus pseudintermedius (MRSP). Then, antibacterial and wound healing activities were evaluated by bacterial cell count, wound contraction, digital capture, and histology. The results show that anisotropic AgNPs gels could eliminate all bacterial cell infected wounds within 7 days, the same as povidone iodine. Wound healing activity was evaluated by wound contraction (%). The results showed 100% wound contraction in groups treated with anisotropic AgNPs gels within 14 days that was not significantly different from povidone iodine and control gel without AgNPs. However, the digital capture of wounds on day 4 showed that anisotropic AgNPs gel prevented pus formation and reduced scar appearance within 21 days. The histology results exhibit improved collagen fiber alignment that supports scar disappearance. In conclusion, these results indicate that anisotropic AgNPs gels are suitable for treating infected wounds. The gel is effective in eliminating bacteria that supports the natural process of wound repair and also causes reduced scar formation.