Dataset Information

Preparation and in Vitro Evaluation of New Composite Mesh Functionalized with Cationic Antimicrobial Peptide.

ABSTRACT: Infection caused by bacteria in hernia repair site is a severe complication, and patients have to undergo a second surgery to remove the infected prosthesis. In this study, we developed a composite biological safe mesh with antibacterial activity. The composite mesh is composed of large pore polypropylene (PP) mesh, poly-caprolactone (PCL) and antimicrobial peptide (PEP-1), which we synthesized in our lab. Fourier transformed infrared (FTIR) spectroscopy was utilized to analyze the functional groups. The surface morphology, in vitro release characters, mechanical properties, antibacterial activities, and in vitro cytotoxicity of modified mesh were evaluated. Results showed that PEP-1 was loaded in fibers successfully and could diffuse from nanofibers to inhibit bacteria (E. coli) growth. However, the modified mesh did not show inhibition to S. aureus. The mechanical properties of fabricated mesh showed no difference with two commercial surgical meshes. What is more, modified mesh was proved to be nontoxic to human dermal fibroblasts, indicating that this method to fabricate meshes with antibacterial activity is feasible and provides a new strategy for the development of surgical meshes.

SUBMITTER: Liu P

PROVIDER: S-EPMC6566986 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature

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Preparation and in Vitro Evaluation of New Composite Mesh Functionalized with Cationic Antimicrobial Peptide.

Liu Pengbi P Chen Nanliang N Jiang Jinhua J Wen Xuejun X

Materials (Basel, Switzerland) 20190523 10

Infection caused by bacteria in hernia repair site is a severe complication, and patients have to undergo a second surgery to remove the infected prosthesis. In this study, we developed a composite biological safe mesh with antibacterial activity. The composite mesh is composed of large pore polypropylene (PP) mesh, poly-caprolactone (PCL) and antimicrobial peptide (PEP-1), which we synthesized in our lab. Fourier transformed infrared (FTIR) spectroscopy was utilized to analyze the functional gr ...[more]

PMID: 31126063

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Project description:Most phages of Gram-negative hosts encode spanins for disruption of the outer membrane, the last step in host lysis. However, bioinformatic analysis indicates that ∼15% of these phages lack a spanin gene, suggesting they have an alternate way of disrupting the OM. Here, we show that the T7-like coliphage phiKT causes the explosive cell lysis associated with spanin activity despite not encoding spanins. A putative lysis cassette cloned from the phiKT late gene region includes the hypothetical novel gene 28 located between the holin and endolysin genes and supports inducible lysis in E. coli K-12. Moreover, induction of an isogenic construct lacking gene 28 resulted in divalent cation-stabilized spherical cells rather than lysis, implicating gp28 in OM disruption. Additionally, gp28 was shown to complement the lysis defect of a spanin-null λ lysogen. Gene 28 encodes a 56-amino acid cationic protein with predicted amphipathic helical structure and is membrane-associated after lysis. Urea and KCl washes did not release gp28 from the particulate, suggesting a strong hydrophobic membrane interaction. Fluorescence microscopy supports membrane localization of the gp28 protein prior to lysis. Gp28 is similar in size, charge, predicted fold, and membrane association to the human cathelicidin antimicrobial peptide LL-37. Synthesized gp28 behaved similar to LL-37 in standard assays mixing peptide and cells to measure bactericidal and inhibitory effects. Taken together, these results indicate that phiKT gp28 is a phage-encoded cationic antimicrobial peptide that disrupts bacterial outer membranes during host lysis and thus establishes a new class of phage lysis proteins, the disruptins. Significance We provide evidence that phiKT produces an antimicrobial peptide for outer membrane disruption during lysis. This protein, designated as a disruptin, is a new paradigm for phage lysis and has no similarities to other known lysis genes. Although many mechanisms have been proposed for the function of antimicrobial peptides, there is no consensus on the molecular basis of membrane disruption. Additionally, there is no established genetic system to support such studies. Therefore, the phiKT disruptin may represent the first genetically tractable antimicrobial peptide, facilitating mechanistic analyses.

Dataset Information

Preparation and in Vitro Evaluation of New Composite Mesh Functionalized with Cationic Antimicrobial Peptide.

Publications

Preparation and in Vitro Evaluation of New Composite Mesh Functionalized with Cationic Antimicrobial Peptide.

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