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Lipid-based liquid crystals as carriers for antimicrobial peptides: Phase behavior and antimicrobial effect
RISE., SP – Sveriges Tekniska Forskningsinstitut, SP Kemi Material och Ytor, Life Science. Chalmers University of Technology, Sweden.ORCID-id: 0000-0003-4742-1702
RISE., SP – Sveriges Tekniska Forskningsinstitut, SP Kemi Material och Ytor, Life Science.ORCID-id: 0000-0002-4122-732x
RISE., SP – Sveriges Tekniska Forskningsinstitut, SP Kemi Material och Ytor, Life Science.
RISE., SP – Sveriges Tekniska Forskningsinstitut, SP Process Development, Analys och fastfas.
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2016 (Engelska)Ingår i: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 32, nr 17, s. 4217-4228Artikel i tidskrift (Refereegranskat) Published
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Abstract [en]

The number of antibiotic-resistant bacteria is increasing worldwide, and the demand for novel antimicrobials is constantly growing. Antimicrobial peptides (AMPs) could be an important part of future treatment strategies of various bacterial infection diseases. However, AMPs have relatively low stability, because of proteolytic and chemical degradation. As a consequence, carrier systems protecting the AMPs are greatly needed, to achieve efficient treatments. In addition, the carrier system also must administrate the peptide in a controlled manner to match the therapeutic dose window. In this work, lyotropic liquid crystalline (LC) structures consisting of cubic glycerol monooleate/water and hexagonal glycerol monooleate/oleic acid/water have been examined as carriers for AMPs. These LC structures have the capability of solubilizing both hydrophilic and hydrophobic substances, as well as being biocompatible and biodegradable. Both bulk gels and discrete dispersed structures (i.e., cubosomes and hexosomes) have been studied. Three AMPs have been investigated with respect to phase stability of the LC structures and antimicrobial effect: AP114, DPK-060, and LL-37. Characterization of the LC structures was performed using small-angle X-ray scattering (SAXS), dynamic light scattering, ζ-potential, and cryogenic transmission electron microscopy (Cryo-TEM) and peptide loading efficacy by ultra performance liquid chromatography. The antimicrobial effect of the LCNPs was investigated in vitro using minimum inhibitory concentration (MIC) and time-kill assay. The most hydrophobic peptide (AP114) was shown to induce an increase in negative curvature of the cubic LC system. The most polar peptide (DPK-060) induced a decrease in negative curvature while LL-37 did not change the LC phase at all. The hexagonal LC phase was not affected by any of the AMPs. Moreover, cubosomes loaded with peptides AP114 and DPK-060 showed preserved antimicrobial activity, whereas particles loaded with peptide LL-37 displayed a loss in its broad-spectrum bactericidal properties. AMP-loaded hexosomes showed a reduction in antimicrobial activity.

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American Chemical Society (ACS), 2016. Vol. 32, nr 17, s. 4217-4228
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Fysikalisk kemi Farmaceutiska vetenskaper
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URN: urn:nbn:se:ri:diva-141DOI: 10.1021/acs.langmuir.6b00338Scopus ID: 2-s2.0-84968912179OAI: oai:DiVA.org:ri-141DiVA, id: diva2:933920
Tillgänglig från: 2016-06-07 Skapad: 2016-06-07 Senast uppdaterad: 2019-06-17Bibliografiskt granskad

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