title: Antifungal nanofibers made by controlled release of sea animal derived peptide.
abstract: Candida albicans is a common human-pathogenic fungal species with the ability to cause several diseases including surface infections. Despite the clear difficulties of Candida control, antimicrobial peptides (AMPs) have emerged as an alternative strategy for fungal control. In this report, different concentrations of antifungal Cm-p1 (Cencritchis muricatus peptide 1) were electrospun into nanofibers for drug delivery. The nanofibers were characterized by mass spectrometry confirming the presence of the peptide on the scaffold. Atomic force microscopy and scanning electronic microscopy were used to measure the diameters, showing that Cm-p1 affects fiber morphology as well as the diameter and scaffold thickness. The Cm-p1 release behavior from the nanofibers demonstrated peptide release from 30 min to three days, leading to effective yeast control in the first 24 hours. Moreover, the biocompatibility of the fibers were evaluated through a MTS assay as well as ROS production by using a HUVEC model, showing that the fibers do not affect cell viability and only nanofibers containing 10% Cm-p1-PVA improved ROS generation. In addition, the secretion of pro-inflammatory cytokines IL-6 and TNF-α by the HUVECs was also slightly modified by the 10% Cm-p1-PVA nanofibers. In conclusion, the electrospinning technique applied here allowed for the manufacture of biodegradable biomimetic nanofibrous extracellular membranes with the ability to control fungal infection.
authors.affiliation: Programa de Pós-Graduação em Patologia Molecular, Universidade de Brasília, Brazil. ocfranco@gmail.com.
authors.forename: Juliane F C
authors.initials: JF
authors.lastname: Viana
authors.forename: Jéssica
authors.initials: J
authors.lastname: Carrijo
authors.forename: Camila G
authors.initials: CG
authors.lastname: Freitas
authors.forename: Arghya
authors.initials: A
authors.lastname: Paul
authors.forename: Jarib
authors.initials: J
authors.lastname: Alcaraz
authors.forename: Cristiano C
authors.initials: CC
authors.lastname: Lacorte
authors.forename: Ludovico
authors.initials: L
authors.lastname: Migliolo
authors.forename: César A
authors.initials: CA
authors.lastname: Andrade
authors.forename: Rosana
authors.initials: R
authors.lastname: Falcão
authors.forename: Nuno C
authors.initials: NC
authors.lastname: Santos
authors.forename: Sónia
authors.initials: S
authors.lastname: Gonçalves
authors.forename: Anselmo J
authors.initials: AJ
authors.lastname: Otero-González
authors.forename: Ali
authors.initials: A
authors.lastname: Khademhosseini
authors.forename: Simoni C
authors.initials: SC
authors.lastname: Dias
authors.forename: Octávio L
authors.initials: OL
authors.lastname: Franco
mesh_terms: D000935:Antifungal Agents / Q000737:chemistry / Q000494:pharmacology; D059001:Aquatic Organisms / Q000737:chemistry*; D002176:Candida albicans / Q000254:growth & development*; D003692:Delayed-Action Preparations / Q000737:chemistry / Q000494:pharmacology; D061307:Human Umbilical Vein Endothelial Cells / Q000166:cytology / Q000378:metabolism*; D006801:Humans; D015850:Interleukin-6 / Q000378:metabolism; D008422:Materials Testing / Q000379:methods; D018625:Microscopy, Atomic Force; D057139:Nanofibers / Q000737:chemistry* / Q000648:ultrastructure; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology; D014409:Tumor Necrosis Factor-alpha / Q000378:metabolism
chemical_list: D000935:Antifungal Agents; D003692:Delayed-Action Preparations; C508600:IL6 protein, human; D015850:Interleukin-6; D010455:Peptides; D014409:Tumor Necrosis Factor-alpha