Mouse ELISA kit[影响因子8.557]

Lingman Ma, Yanrong Wang, Mengxiao Wang, Yuwei Tian, Wei Kang, Hanhan Liu,Hui Wang, Jie Dou*, Changlin Zhou
Cbf-14, a cationic peptide derived from a cathelin-like domain, was designed by inserting the highly ahelical sequence RLLR into an antibacterial sequence and deleting the inactive amino acids in Cbf-K16.Clinical penicillin-resistant isolates as well as NDM-1-carrying Escherichia coli and a correspondingly infected mice model were employed to evaluate Cbf-14 antibacterial activity. The results showed that Cbf-14 possessed potent antimicrobial effects with an MIC of 8e64 mg/ml, and killed almost all bacteria within 240 min. Cbf-14-treated mice achieved an 80% survival rate and approximate 2.5 log unit reduction in CFU in tissues; additionally, this peptide significantly suppressed the production of proinflammatory cytokines by the disaggregation of lipopolysaccharide (LPS), suggesting its antiinflammatory effects. Furthermore, Cbf-14, concentration higher than 2
MIC value, increased membrane uptake to NPN and PI dye by 96.2% and 63.7%, respectively, neutralised the negative zeta potential of LPS and bacteria surface, and induced 100% leakage of liposome-entrapped calcein and cytoplasmic membrane disruption of E. coli, indicating obvious membrane permeation. Finally, it bound to DNA and respectively evoked 85.0% and 63.3% inhibition of gene replication and protein expression of NDM-1 at sub-MIC concentration in E. coli BL21 (DE3)-NDM-1. These data indicated that Cbf-14 possessed effective antimicrobial activity against penicillin-resistant bacteria in vitro/vivo through membrane disruption, DNA binding, down-regulating NDM-1 expression by plasmid replication inhibition, and antiinflammatory activity by LPS disaggregation, suggesting a potential anti-infective clinical agent【完整论文请戳标题】Effective antimicrobial activity of Cbf-14, derived from a cathelin-like domain, against penicillin-resistant bacteria