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- 저자 : Lingman Ma (검색결과 2 건)
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Jing Jin,Yuanjin Chen,Dechuan Wang,Lingman Ma,Min Guo,Changlin Zhou,Jie Dou 대한약학회 2018 Archives of Pharmacal Research Vol.41 No.6
Baicalin was identified as a neuraminidase (NA)inhibitor displaying anti-influenza A virus (IAV) activity. However, its poor solubility in saline has limited its use inthe clinic. We generated sodium baicalin and showed that itexhibited greatly increased solubility in saline. Its efficacyagainst oseltamivir-resistant mutant A/FM/1/47-H275Y(H1N1-H275Y) was evaluated in vitro and in vivo. Resultsshowed that 10 lM of sodium baicalin inhibited A/FM/1/47 (H1N1), A/Beijing/32/92 (H3N2) and H1N1-H275Y inMDCK cells in a dose-dependent manner, with inhibitoryrates of 83.9, 75.9 and 47.7%, respectively. Intravenousadministration of sodium baicalin at 100 mg/kg/d enabledthe survival of 20% of H1N1-H275Y-infected mice. Thetreatment alleviated body weight loss and lung injury. Moreover, sodium baicalin exerted a clear inhibitory effecton NAs. The IC50 values of sodium baicalin against H1N1-H275Y and cells-expressing A/Anhui/1/2013-R294K(H7N9-R294K) NA protein (N9-R294K) were 214.4 lMand 216.3 lM. Direct interactions between sodium baicalinand NA were observed, and we simulated the interactionsof sodium baicalin with N9-R294K and N9 near the activesites of OC-N9-R294K and OC-N9. The residues responsiblefor the sodium baicalin-N9-R294K and sodiumbaicalin-N9 interactions were the same, confirming thatsodium baicalin exerts effects on wild-type and oseltamivir-resistant viral strains.
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Wang Liping,Liu Xiaoyun,Ye Xinyue,Zhou Chenyu,Zhao Wenxuan,Zhou Changlin,Ma Lingman 한국미생물학회 2022 The journal of microbiology Vol.60 No.1
The poor stability of peptides against trypsin largely limits their development as potential antibacterial agents. Here, to obtain a peptide with increased trypsin stability and potent antibacterial activity, TICbf-14 derived from the cationic peptide Cbf-14 was designed by the addition of disulfide-bridged hendecapeptide (CWTKSIPPKPC) loop. Subsequently, the trypsin stability and antimicrobial and antibiofilm activities of this peptide were evaluated. The possible mechanisms underlying its mode of action were also clarified. The results showed that TICbf-14 exhibited elevated trypsin inhibitory activity and effectively mitigated lung histopathological damage in bacteria-infected mice by reducing the bacterial counts, further inhibiting the systemic dissemination of bacteria and host inflammation. Additionally, TICbf-14 significantly repressed bacterial swimming motility and notably inhibited biofilm formation. Considering the mode of action, we observed that TICbf-14 exhibited a potent membrane-disruptive mechanism, which was attributable to its destructive effect on ionic bridges between divalent cations and LPS of the bacterial membrane. Overall, TICbf-14, a bifunctional peptide with both antimicrobial and trypsin inhibitory activity, is highly likely to become an ideal candidate for drug development against bacteria.
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