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Electrospray loading and release of hydrophobic gramicidin in polyester microparticles

AutorMaione, Silvana; Valle, Luis J. del; Pérez-Madrigal, Maria M.; Cativiela, Carlos ; Puiggalí, Jordi; Alemán, Carlos
Fecha de publicación2016
EditorRoyal Society of Chemistry (Great Britain)
CitaciónRSC Advances 6(77): 73045-73055 (2016)
ResumenGramicidin (GA), a very hydrophobic pentadecapeptide with important biological activities (i.e. in addition to its well-known antimicrobial and antibiotic activities, GA has been recently identified as a potent therapeutic agent against different carcinomas), has been loaded by electrospraying in poly(tetramethylene succinate) (PE44), a biodegradable and biocompatible aliphatic polyester. Microspheres (average diameter: 5.0 ± 0.7 μm) were successfully obtained from the mixture of GA and PE44 solutions in ethanol and chloroform, respectively. The loading of the peptide, which has been proved by FTIR and X-ray photoelectron spectroscopies, essentially occurred at the surface of the microspheres, as was reflected by scanning electron microscopy micrographs and atomic force microscopy phase images. In spite of this, the thermal stability of the polyester matrix remained essentially unaltered, even though the wettability decreased. The release of GA in phosphate buffer saline (PBS) was limited by the very low solubility of the peptide in aqueous solution, a fast burst effect followed by the establishment of equilibrium after 5 days of being observed in this hydrophilic environment. The release behaviour was very different when the hydrophilicity of the medium was reduced by adding ethanol. In this case, a very fast but sustained release was identified during the first few hours. On the other hand, biological tests have demonstrated that GA retains its antimicrobial activity after loading and does not alter the biocompatibility of PE44. Our results prove that, despite its hydrophobicity and relatively large number of residues, the loading of GA in a polymeric matrix represents an alternative strategy for the release of this versatile peptide in cancer therapy.
URIhttp://hdl.handle.net/10261/154795
DOI10.1039/C6RA11056H
Identificadoresdoi: 10.1039/C6RA11056H
e-issn: 2046-2069
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