A comparative analysis of antibacterial properties and inflammatory responses for the KR-12 peptide on titanium and PEGylated titanium surfaces. Issue 55 (10th July 2017)
- Record Type:
- Journal Article
- Title:
- A comparative analysis of antibacterial properties and inflammatory responses for the KR-12 peptide on titanium and PEGylated titanium surfaces. Issue 55 (10th July 2017)
- Main Title:
- A comparative analysis of antibacterial properties and inflammatory responses for the KR-12 peptide on titanium and PEGylated titanium surfaces
- Authors:
- Nie, Bin'en
Long, Teng
Li, Hui
Wang, Xiaojie
Yue, Bing - Abstract:
- Abstract : Covalent KR-12 peptide immobilisation on the Ti surface with a grafted PEG spacer showed remarkable antibacterial properties and reduced macrophage inflammatory responses. Abstract : Covalent immobilisation of antimicrobial peptides on titanium (Ti) surfaces has been widely performed to inhibit bacterial adhesion and biofilm formation, however, it is unclear whether a spacer is necessary in this process for anti-bacteria adhesion, while still exhibiting good biocompatibility. We investigated the antibacterial properties and inflammatory response of Ti and PEGylated Ti with covalently immobilized KR-12 peptide on the surfaces. The KR-12 peptide was derived from LL-37, which is bactericidal and bacteriostatic in solution. Successful covalent immobilisation was determined by X-ray photoelectron spectrometry, contact angle measurements, and atomic force microscopy. KR-12 incorporation significantly decreased the bacterial adhesion to the Ti surface. Compared to the Ti-KR-12, the KR-12 immobilisation via a PEG spacer increased anti-microbial efficiency and reduced in vitro adhesion and biofilm formation of Staphylococcus epidermidis . Activated macrophages deprived from THP-1 cells with long filopodia were observed on the titanium surface, which was in agreement with increased TNF-α and IL-1β secretion. The KR-12-modified Ti surface and PEGylated Ti surface significantly decreased TNF-α and IL-1β secretion and macrophages remained in inactivated round states. TheAbstract : Covalent KR-12 peptide immobilisation on the Ti surface with a grafted PEG spacer showed remarkable antibacterial properties and reduced macrophage inflammatory responses. Abstract : Covalent immobilisation of antimicrobial peptides on titanium (Ti) surfaces has been widely performed to inhibit bacterial adhesion and biofilm formation, however, it is unclear whether a spacer is necessary in this process for anti-bacteria adhesion, while still exhibiting good biocompatibility. We investigated the antibacterial properties and inflammatory response of Ti and PEGylated Ti with covalently immobilized KR-12 peptide on the surfaces. The KR-12 peptide was derived from LL-37, which is bactericidal and bacteriostatic in solution. Successful covalent immobilisation was determined by X-ray photoelectron spectrometry, contact angle measurements, and atomic force microscopy. KR-12 incorporation significantly decreased the bacterial adhesion to the Ti surface. Compared to the Ti-KR-12, the KR-12 immobilisation via a PEG spacer increased anti-microbial efficiency and reduced in vitro adhesion and biofilm formation of Staphylococcus epidermidis . Activated macrophages deprived from THP-1 cells with long filopodia were observed on the titanium surface, which was in agreement with increased TNF-α and IL-1β secretion. The KR-12-modified Ti surface and PEGylated Ti surface significantly decreased TNF-α and IL-1β secretion and macrophages remained in inactivated round states. The grafting of a PEG spacer prior to KR-12 immobilisation on the Ti surface improved the antibacterial properties and reduced macrophage activation, and may also decrease overall inflammatory responses. Thus, this approach showed the potential to biofunctionalize Ti for anti-bacteria adhesion and reducing macrophage inflammation. … (more)
- Is Part Of:
- RSC advances. Volume 7:Issue 55(2017)
- Journal:
- RSC advances
- Issue:
- Volume 7:Issue 55(2017)
- Issue Display:
- Volume 7, Issue 55 (2017)
- Year:
- 2017
- Volume:
- 7
- Issue:
- 55
- Issue Sort Value:
- 2017-0007-0055-0000
- Page Start:
- 34321
- Page End:
- 34330
- Publication Date:
- 2017-07-10
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c7ra05538b ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 2783.xml