Cargando…
Antibacterial Activity on Orthopedic Clinical Isolates and Cytotoxicity of the Antimicrobial Peptide Dadapin-1
In orthopedic surgery, biomaterial-associated infections represent a complication of serious concern. Most promising strategies to prevent these infections currently rely on the use of anti-infective biomaterials. Desirably, in anti-infective biomaterials, the antibacterial properties should be achi...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9821071/ https://www.ncbi.nlm.nih.gov/pubmed/36614222 http://dx.doi.org/10.3390/ijms24010779 |
_version_ | 1784865610485727232 |
---|---|
author | Campoccia, Davide Montanaro, Lucio Ravaioli, Stefano Mariani, Valentina Bottau, Giulia De Donno, Andrea Arciola, Carla Renata |
author_facet | Campoccia, Davide Montanaro, Lucio Ravaioli, Stefano Mariani, Valentina Bottau, Giulia De Donno, Andrea Arciola, Carla Renata |
author_sort | Campoccia, Davide |
collection | PubMed |
description | In orthopedic surgery, biomaterial-associated infections represent a complication of serious concern. Most promising strategies to prevent these infections currently rely on the use of anti-infective biomaterials. Desirably, in anti-infective biomaterials, the antibacterial properties should be achieved by doping, grafting, or coating the material surfaces with molecules that are alternative to conventional antibiotics and exhibit a potent and highly specific activity against bacteria, without altering the biocompatibility. Antimicrobial peptides (AMPs) are among the most interesting candidate molecules for this biomaterial functionalization. Here, the potential expressed by the recently discovered peptide Dadapin-1 was explored by assaying its MIC, MBIC and MBC on clinical strains of relevant bacterial species isolated from orthopedic infections and by assessing its cytotoxicity on the human osteoblast-like MG63 cells. When appropriately tested in diluted Mueller Hinton Broth II (MHB II), Dadapin-1 exhibited significant antibacterial properties. MIC values were in the range of 3.1–6.2 µM for the gram-positive bacteria Staphylococcus aureus, Staphylococcus epidermidis, and Staphylococcus warneri, and 12.4–24.9 µM for the gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa. Interestingly, the peptide was found non-cytotoxic, with an IC50 exceeding the highest concentration tested of 179 µM. Overall, Dadapin-1 expresses considerable potential for future application in the production of anti-infective biomaterials. |
format | Online Article Text |
id | pubmed-9821071 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-98210712023-01-07 Antibacterial Activity on Orthopedic Clinical Isolates and Cytotoxicity of the Antimicrobial Peptide Dadapin-1 Campoccia, Davide Montanaro, Lucio Ravaioli, Stefano Mariani, Valentina Bottau, Giulia De Donno, Andrea Arciola, Carla Renata Int J Mol Sci Article In orthopedic surgery, biomaterial-associated infections represent a complication of serious concern. Most promising strategies to prevent these infections currently rely on the use of anti-infective biomaterials. Desirably, in anti-infective biomaterials, the antibacterial properties should be achieved by doping, grafting, or coating the material surfaces with molecules that are alternative to conventional antibiotics and exhibit a potent and highly specific activity against bacteria, without altering the biocompatibility. Antimicrobial peptides (AMPs) are among the most interesting candidate molecules for this biomaterial functionalization. Here, the potential expressed by the recently discovered peptide Dadapin-1 was explored by assaying its MIC, MBIC and MBC on clinical strains of relevant bacterial species isolated from orthopedic infections and by assessing its cytotoxicity on the human osteoblast-like MG63 cells. When appropriately tested in diluted Mueller Hinton Broth II (MHB II), Dadapin-1 exhibited significant antibacterial properties. MIC values were in the range of 3.1–6.2 µM for the gram-positive bacteria Staphylococcus aureus, Staphylococcus epidermidis, and Staphylococcus warneri, and 12.4–24.9 µM for the gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa. Interestingly, the peptide was found non-cytotoxic, with an IC50 exceeding the highest concentration tested of 179 µM. Overall, Dadapin-1 expresses considerable potential for future application in the production of anti-infective biomaterials. MDPI 2023-01-02 /pmc/articles/PMC9821071/ /pubmed/36614222 http://dx.doi.org/10.3390/ijms24010779 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Campoccia, Davide Montanaro, Lucio Ravaioli, Stefano Mariani, Valentina Bottau, Giulia De Donno, Andrea Arciola, Carla Renata Antibacterial Activity on Orthopedic Clinical Isolates and Cytotoxicity of the Antimicrobial Peptide Dadapin-1 |
title | Antibacterial Activity on Orthopedic Clinical Isolates and Cytotoxicity of the Antimicrobial Peptide Dadapin-1 |
title_full | Antibacterial Activity on Orthopedic Clinical Isolates and Cytotoxicity of the Antimicrobial Peptide Dadapin-1 |
title_fullStr | Antibacterial Activity on Orthopedic Clinical Isolates and Cytotoxicity of the Antimicrobial Peptide Dadapin-1 |
title_full_unstemmed | Antibacterial Activity on Orthopedic Clinical Isolates and Cytotoxicity of the Antimicrobial Peptide Dadapin-1 |
title_short | Antibacterial Activity on Orthopedic Clinical Isolates and Cytotoxicity of the Antimicrobial Peptide Dadapin-1 |
title_sort | antibacterial activity on orthopedic clinical isolates and cytotoxicity of the antimicrobial peptide dadapin-1 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9821071/ https://www.ncbi.nlm.nih.gov/pubmed/36614222 http://dx.doi.org/10.3390/ijms24010779 |
work_keys_str_mv | AT campocciadavide antibacterialactivityonorthopedicclinicalisolatesandcytotoxicityoftheantimicrobialpeptidedadapin1 AT montanarolucio antibacterialactivityonorthopedicclinicalisolatesandcytotoxicityoftheantimicrobialpeptidedadapin1 AT ravaiolistefano antibacterialactivityonorthopedicclinicalisolatesandcytotoxicityoftheantimicrobialpeptidedadapin1 AT marianivalentina antibacterialactivityonorthopedicclinicalisolatesandcytotoxicityoftheantimicrobialpeptidedadapin1 AT bottaugiulia antibacterialactivityonorthopedicclinicalisolatesandcytotoxicityoftheantimicrobialpeptidedadapin1 AT dedonnoandrea antibacterialactivityonorthopedicclinicalisolatesandcytotoxicityoftheantimicrobialpeptidedadapin1 AT arciolacarlarenata antibacterialactivityonorthopedicclinicalisolatesandcytotoxicityoftheantimicrobialpeptidedadapin1 |