Abstract：
:Antimicrobial peptides (AMPs) are essential host defence molecules found in a wide variety of species and are promising antibacterial therapeutic candidates. Focusing on the human cathelicidin peptide LL-37, the aim of the present study was to explore the mechanisms of action and antimicrobial activities of a library of LL-37 fragments using Burkholderia thailandensis E264 as a model. The results revealed that IG-19 was the shortest fragment within LL-37 that exhibited antibacterial activity. LL-31, missing six residues at the C-terminus of LL-37, exhibited the strongest killing effect. Freeze-fracture electron microscopy of bacterial cells treated with either LL-37 or LL-31 revealed irregular bacterial surfaces with bleb projections, indicating that these peptides disrupted the integrity of the membrane. In addition, these peptides induced leakage of cell components, including nucleotides and even proteins. Altogether, the results obtained indicate the potential of using LL-31 as a new AMP to combat Burkholderia spp.
journal_name
Int J Antimicrob Agentsjournal_title
International journal of antimicrobial agentsauthors
Kanthawong S,Bolscher JG,Veerman EC,van Marle J,Nazmi K,Wongratanacheewin S,Taweechaisupapong Sdoi
10.1016/j.ijantimicag.2010.06.031subject
Has Abstractpub_date
2010-11-01 00:00:00pages
447-52issue
5eissn
0924-8579issn
1872-7913pii
S0924-8579(10)00272-4journal_volume
36pub_type
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