Inhibitory effect of short cationic homopeptides against Gram-negative bacteria View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2016-06

AUTHORS

Patricio Carvajal-Rondanelli, Mónica Aróstica, Sergio Hernan Marshall, Fernando Albericio, Claudio Andrés Álvarez, Claudia Ojeda, Luis Felipe Aguilar, Fanny Guzmán

ABSTRACT

Previous work demonstrated that Lys homopeptides with an odd number of residues (9, 11 and 13) were capable of inhibiting the growth of Gram-positive bacteria in a broader spectrum and more efficiently than those with an even number of Lys residues or Arg homopeptides of the same size. Indeed, all Gram-positive bacteria tested were totally inhibited by 11-residue Lys homopeptides. In the present work, a wide variety of Gram-negative bacteria were used to evaluate the inhibitory activity of chemically synthesized homopeptides of L-Lys and L-Arg ranging from 7 to 14 residues. Gram-negative bacteria were comparatively more resistant than Gram-positive bacteria to Lys homopeptides with an odd number of residues, but exhibited a similar inhibition pattern than on Gram-positive bacteria. CD spectra for the odd-numbered Lys homopeptides in anionic lipid dimyristoylphosphatidylglycerol, and Escherichia coli membrane extract increased polyproline II content, as compared to those measured in phosphate buffer solution. Lys and Arg homopeptides were covalently linked to rhodamine to visualize the peptide interactions with E. coli cells using confocal laser scanning microscopy. Analysis of Z-stack images showed that Arg homopeptides indeed appear to be localized intracellularly, while the Lys homopeptide is localized exclusively on the plasma membrane. Moreover, these Lys homopeptides induced membrane disruption since the Sytox fluorophore was able to bind to the DNA in E. coli cultures. More... »

PAGES

1445-1456

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00726-016-2198-z

DOI

http://dx.doi.org/10.1007/s00726-016-2198-z

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1012555076

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26922474


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RDF/XML is a standard XML format for linked data.

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288 Instituto de Biología, Pontificia Universidad Católica de Valparaíso, Av. Brasil, 2950, Valparaíso, Chile
289 Instituto de Química, Pontificia Universidad Católica de Valparaíso, Av. Brasil, 2950, Valparaíso, Chile
290 Núcleo de Biotecnología Curauma, Pontificia Universidad Católica de Valparaíso, Av. Brasil, 2950, Valparaíso, Chile
291 rdf:type schema:Organization
 




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