Abstract:
:Lactocin 705 is a bacteriocin whose activity depends upon the complementation of two peptides, termed Lac705alpha and Lac705beta. Neither Lac705alpha nor Lac705beta displayed bacteriocin activity by itself when the growth of sensitive cells was monitored. To obtain molecular insights into the lactocin 705 mechanism of action, Fourier transform infrared spectroscopy was used to investigate the interactions of each peptide (Lac705alpha and Lac705beta) with dipalmitoylphosphatidylcholine liposomal membranes. Both peptides show the ability to interact with the zwitterionic membrane but at different bilayer levels. While Lac705alpha interacts with the interfacial region inducing dehydration, Lac705beta peptide interacts with only the hydrophobic core. This paper presents the first experimental evidence that supports the hypothesis that Lac705alpha and Lac705beta peptides could form a transmembrane oligomer. From the obtained results, a mechanism of action of lactocin 705 on membrane systems is proposed. The component Lac705alpha could induce the dehydration of the bilayer interfacial region, and the Lac705beta peptide could insert in the hydrophobic region of the membrane where the peptide has adequate conditions to achieve the oligomerization.
journal_name
Appl Environ Microbioljournal_title
Applied and environmental microbiologyauthors
Castellano P,Vignolo G,Farías RN,Arrondo JL,Chehín Rdoi
10.1128/AEM.01293-06subject
Has Abstractpub_date
2007-01-01 00:00:00pages
415-20issue
2eissn
0099-2240issn
1098-5336pii
AEM.01293-06journal_volume
73pub_type
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