Combined experimental and in silico elucidation of KP27 endolysin reveals a phage derived antibacterial with pH and thermal robustness

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来源: Nature 关键字: computational biology
发布时间: 2025-12-08 23:53
摘要:

KP27 endolysin, derived from Klebsiella phage, exhibits potent antibacterial activity against multidrug-resistant bacteria, including Staphylococcus aureus and Escherichia coli. Characterization studies reveal its stability across various pH levels and temperatures, with optimal enzymatic activity at neutral pH. The endolysin's mechanism involves cleaving peptidoglycan bonds, leading to rapid bacterial lysis. Its favorable safety profile, demonstrated by minimal hemolytic activity, positions KP27 as a promising candidate for therapeutic applications in combating antibiotic resistance.

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关键证据

KP27 demonstrated dose-dependent bactericidal activity, reducing Staphylococcus aureus and Escherichia coli viability by up to 80% and 65%, respectively.
The enzyme maintains optimal activity and stable secondary and tertiary structures around neutral to slightly alkaline pH.
KP27 exhibits considerable thermal stability, retaining activity at temperatures up to 80 °C.

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KP27 endolysin, derived from Klebsiella phage, exhibits potent antibacterial activity against multidrug-resistant bacteria, including Staphylococcus aureus and Escherichia coli. Characterization studies reveal its stability across various pH levels and temperatures, with optimal enzymatic activity at neutral pH. The endolysin's mechanism involves cleaving peptidoglycan bonds, leading to rapid bacterial lysis. Its favorable safety profile, demonstrated by minimal hemolytic activity, positions KP27 as a promising candidate for therapeutic applications in combating antibiotic resistance.

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