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1.
Vaccine ; 2024 Jun 03.
Article in English | MEDLINE | ID: mdl-38834431

ABSTRACT

Globally, influenza poses a substantial threat to public health, serving as a major contributor to both morbidity and mortality. The current vaccines for seasonal influenza are not optimal. A novel recombinant hemagglutinin (rHA) protein-based quadrivalent seasonal influenza vaccine, SCVC101, has been developed. SCVC101-S contains standard dose protein (15µg of rHA per virus strain) and an oil-in-water adjuvant, CD-A, which enhances the immunogenicity and cross-protection of the vaccine. Preclinical studies in mice, rats, and rhesus macaques demonstrate that SCVC101-S induces robust humoral and cellular immune responses, surpassing those induced by commercially available vaccines. Notably, a single injection with SCVC101-S can induce a strong immune response in macaques, suggesting the potential for a standard-dose vaccination with a recombinant protein influenza vaccine. Furthermore, SCVC101-S induces cross-protection immune responses against heterologous viral strains, indicating broader protection than current vaccines. In conclusion, SCVC101-S has demonstrated safety and efficacy in preclinical settings and warrants further investigation in human clinical trials. Its potential as a valuable addition to the vaccines against seasonal influenza, particularly for the elderly population, is promising.

2.
J Cosmet Sci ; 64(2): 99-110, 2013.
Article in English | MEDLINE | ID: mdl-23578833

ABSTRACT

Tyrosinase inhibitors from natural plants are currently attracting great interest. In this study, vanillic acid (VA) from red globe amaranth flower was identified as an effective tyrosinase inhibitor. The 50% inhibitory concentration values of VA were 0.53 and 0.63 mg/ml for the monophenolase and diphenolase activities of tyrosinase, respectively. VA did not function as a simple copper chelator, and it did not induce detectable changes in the enzyme conformation. An investigation into the interaction between VA and tyrosinase by docking method revealed that VA was bound to residues at the entrance to the dicopper center. This suggests that VA could strongly inhibit tyrosinase activity by hampering the binding of substrates to tyrosinase. Because of the stability of the complex, VA hindered binding of monophenol substrates better than that of diphenol substrates, which resulted in different inhibitory efficacies. A study of the mechanism of tyrosinase inhibition provided new evidence to elucidate the molecular mechanism of depigmentation by red globe amaranth plant.


Subject(s)
Amaranthus/chemistry , Bacterial Proteins/chemistry , Copper/chemistry , Fungal Proteins/antagonists & inhibitors , Monophenol Monooxygenase/antagonists & inhibitors , Plant Extracts/chemistry , Vanillic Acid/chemistry , Catalytic Domain , Enzyme Assays , Fungal Proteins/chemistry , Kinetics , Molecular Docking Simulation , Monophenol Monooxygenase/chemistry , Oxidation-Reduction , Protein Binding , Structural Homology, Protein , Vanillic Acid/isolation & purification
3.
Acta Crystallogr Sect E Struct Rep Online ; 67(Pt 4): o974-5, 2011 Apr 01.
Article in English | MEDLINE | ID: mdl-21754235

ABSTRACT

The title compound, C(31)H(44)N(3)O(10) (+)·Cl(-)·CH(4)O, is the methanol solvate of 8-benzo-yloxy-,9,11,11a-tetra-hydroxy-6,10,13-trimeth-oxy-3-meth-oxy-methyl-1-methyl-tetra-deca-hydro-1H-3,6a,12-(epiethane-1,1,2-tri-yl)-7,9-methanona-phtho[2,3-b]azocin-1-ium chloride, the amine-protonated hydro-chloride of 14-benzoyl-mesaconine hydro-chloride. The cation has an aconitine carbon skeleton with four six-membered rings of which three display chair conformations and one a boat conformation, and two five-membered rings with envelope conformations. In the crystal, the components are connected into an infinite chain by inter- and intra-molecular O-H⋯O, N-H⋯O and O-H⋯Cl hydrogen bonds.

4.
Anim Sci J ; 82(1): 122-6, 2011 Feb.
Article in English | MEDLINE | ID: mdl-21269370

ABSTRACT

Yak butter in Tsinghai-Tibet Plateau possesses the characters of high energy, abundant alimentation and a special flavor with certain medical and health care functions. In this paper the organoleptic flavor of yak butter was estimated, and 28 kinds of substance with different flavors were identified with the technique of coupling gas chromatography to mass spectroscopy (GC-MS). The results showed that there are many microorganisms in yak butter with natural inoculation, which contribute to the formation of its special flavors. It was found that three of these 15 microorganisms, identified as Saccharomycetaceae, Penicillium and Asperillus separately, contributed the most to flavors. The microorganisms are expected to be applied in the food industry, especially to produce dairy food with the unique flavor of yak butter.


Subject(s)
Aspergillus/isolation & purification , Butter/analysis , Butter/microbiology , Cultured Milk Products/chemistry , Cultured Milk Products/microbiology , Food Analysis , Food Microbiology , Penicillium/isolation & purification , Saccharomycetales/isolation & purification , Taste , Animals , Cattle , Fermentation , Gas Chromatography-Mass Spectrometry , Humans , Milk , Tibet
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