Journal: ACS Omega

Article Title: Enzyme-Based Antiviral Potential of Cinnamomum verum J. Presl. Essential Oil and Its Major Component ( E )-Cinnamaldehyde

doi: 10.1021/acsomega.3c09595

Figure Lengend Snippet: (a) Cinnamaldehyde prefers to bind in the S1 site of ACE2 subdomain II. The zinc center located in subdomain I can be seen in the background. Black dotted lines represent hydrogen bonds. (b) The binding mode of cinnamaldehyde for neuraminidase features substrate-like bidentate hydrogen bonding with Arg 118. To some extent, the binding also is similar to that of oseltamivir. (c) Hydrophobic interaction of cinnamaldehyde with Gln 438 in the S3 subsite of TMPRSS2 away from the catalytic triad: Ser 441, His 296, and Asp 345.

Article Snippet: TMPRSS2 and Neuraminidase kits were purchased from Abcam (BPS Bioscience 78083, San Diego, CA) and Sigma-Aldrich (MAK121, Darmstadt, Germany), respectively.

Techniques: Binding Assay

Journal: ACS Omega

Article Title: Enzyme-Based Antiviral Potential of Cinnamomum verum J. Presl. Essential Oil and Its Major Component ( E )-Cinnamaldehyde

doi: 10.1021/acsomega.3c09595

Figure Lengend Snippet: Enzyme Inhibitory Activity of C. verum Essential Oil and ( E )-cinnamaldehyde

Article Snippet: TMPRSS2 and Neuraminidase kits were purchased from Abcam (BPS Bioscience 78083, San Diego, CA) and Sigma-Aldrich (MAK121, Darmstadt, Germany), respectively.

Techniques: Activity Assay, Enzyme Inhibition Assay, Control

Journal: ACS Omega

Article Title: Enzyme-Based Antiviral Potential of Cinnamomum verum J. Presl. Essential Oil and Its Major Component ( E )-Cinnamaldehyde

doi: 10.1021/acsomega.3c09595

Figure Lengend Snippet: Binding Energies of Cinnamaldehyde for the Target Enzymes

Article Snippet: TMPRSS2 and Neuraminidase kits were purchased from Abcam (BPS Bioscience 78083, San Diego, CA) and Sigma-Aldrich (MAK121, Darmstadt, Germany), respectively.

Techniques: Binding Assay

Journal: The Journal of Biological Chemistry

Article Title: Hydrolysis of Secreted Sialoglycoprotein Immunoglobulin A (IgA) in ex Vivo and Biochemical Models of Bacterial Vaginosis *

doi: 10.1074/jbc.M111.278135

Figure Lengend Snippet: Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using 4MUSia. Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.

Article Snippet: Fluorogenic sialidase substrate 2–4-methylumbelliferyl-α- d - N -acetylneuraminic acid sodium salt (4MUSia) from Gold BioTechnology was dissolved at 10 m m in water, aliquotted, and frozen at −80 °C.

Techniques: Activity Assay, Staining, Concentration Assay

Journal: The Journal of Biological Chemistry

Article Title: Hydrolysis of Secreted Sialoglycoprotein Immunoglobulin A (IgA) in ex Vivo and Biochemical Models of Bacterial Vaginosis *

doi: 10.1074/jbc.M111.278135

Figure Lengend Snippet: BV sialidases act on sialic acids presented in multiple contexts relevant to the reproductive mucosa. BV specimens containing high levels of sialidase were incubated alongside matched controls (n = 14 each) with macromolecules bearing terminal sialic acids in different contexts. Released sialic acid was quantified by derivatization and HPLC as described in “Experimental Procedures” to assess the ability of BV sialidases to cleave different types of sialic acid-containing substrates. All of the data were normalized to total sialic acid (Neu5Ac) released by digestion with A. ureafaciens sialidase, shown in separate experiments to result in complete release as compared with acid hydrolysis. All of the substrates tested, including 2,3-linked sialic acids from the group B Streptococcus (GBS) capsule and primarily O-linked sialo-glycans from bovine submaxillary mucin (BSM), were desialylated to near completion by BV samples, whereas control specimens had little evidence of sialic acid hydrolysis. The Mann-Whitney U test was used to examine statistical significance (p < 0.0001 for all substrates; inset). The levels of sialidase activity (4MUSia) indicated for each sample are initial rates normalized relative to the sample with highest activity level.

Article Snippet: Fluorogenic sialidase substrate 2–4-methylumbelliferyl-α- d - N -acetylneuraminic acid sodium salt (4MUSia) from Gold BioTechnology was dissolved at 10 m m in water, aliquotted, and frozen at −80 °C.

Techniques: Incubation, MANN-WHITNEY, Activity Assay