Antibacterial Properties of hLf1–11 Peptide onto Titanium Surfaces: A Comparison Study Between Silanization and Surface Initiated Polymerization
Dental implant failure can be associated with infections that develop into peri-implantitis. In order to reduce biofilm formation, several strategies focusing on the use of antimicrobial peptides (AMPs) have been studied. To covalently immobilize these molecules onto metallic substrates, several tec...
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description | Dental implant failure can be associated with infections that develop into peri-implantitis. In order to reduce biofilm formation, several strategies focusing on the use of antimicrobial peptides (AMPs) have been studied. To covalently immobilize these molecules onto metallic substrates, several techniques have been developed, including silanization and polymer brush prepared by surface-initiated atom transfer radical polymerization (ATRP), with varied peptide binding yield and antibacterial performance. The aim of the present study was to compare the efficiency of these methods to immobilize the lactoferrin-derived hLf1–11 antibacterial peptide onto titanium, and evaluate their antibacterial activity in vitro. Smooth titanium samples were coated with hLf1–11 peptide under three different conditions: silanization with 3-aminopropyltriethoxysilane (APTES), and polymer brush based coatings with two different silanes. Peptide presence was determined by X-ray photoelectron spectroscopy, and the mechanical stability of the coatings was studied under ultrasonication. The LDH assays confirmed that HFFs viability and proliferation were no affected by the treatments. The in vitro antibacterial properties of the modified surfaces were tested with two oral strains (Streptococcus sanguinis and Lactobacillus salivarius) showing an outstanding reduction. A higher decrease in bacterial attachment was noticed when samples were modified by ATRP methods compared to silanization. This effect is likely due to the capacity to immobilize more peptide on the surfaces using polymer brushes and the nonfouling nature of polymer PDMA segment. |
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In order to reduce biofilm formation, several strategies focusing on the use of antimicrobial peptides (AMPs) have been studied. To covalently immobilize these molecules onto metallic substrates, several techniques have been developed, including silanization and polymer brush prepared by surface-initiated atom transfer radical polymerization (ATRP), with varied peptide binding yield and antibacterial performance. The aim of the present study was to compare the efficiency of these methods to immobilize the lactoferrin-derived hLf1–11 antibacterial peptide onto titanium, and evaluate their antibacterial activity in vitro. Smooth titanium samples were coated with hLf1–11 peptide under three different conditions: silanization with 3-aminopropyltriethoxysilane (APTES), and polymer brush based coatings with two different silanes. Peptide presence was determined by X-ray photoelectron spectroscopy, and the mechanical stability of the coatings was studied under ultrasonication. The LDH assays confirmed that HFFs viability and proliferation were no affected by the treatments. The in vitro antibacterial properties of the modified surfaces were tested with two oral strains (Streptococcus sanguinis and Lactobacillus salivarius) showing an outstanding reduction. A higher decrease in bacterial attachment was noticed when samples were modified by ATRP methods compared to silanization. This effect is likely due to the capacity to immobilize more peptide on the surfaces using polymer brushes and the nonfouling nature of polymer PDMA segment.</description><identifier>ISSN: 1525-7797</identifier><identifier>EISSN: 1526-4602</identifier><identifier>DOI: 10.1021/bm501528x</identifier><identifier>PMID: 25545728</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Anti-Bacterial Agents - chemistry ; Anti-Bacterial Agents - pharmacology ; antimicrobial peptides ; attachment ; brushes ; Cell Survival - drug effects ; Cell Survival - physiology ; cell-adhesive ; Cells, Cultured ; Dental Implants ; Enginyeria dels materials ; escherichia-coli ; Humans ; Implants artificials ; in-vitro ; Lactobacillus salivarius ; lactoferricin-b ; Lactoferrin - chemistry ; Lactoferrin - pharmacology ; Male ; Peptide Fragments - chemistry ; Peptide Fragments - pharmacology ; Polymerization ; roughness ; Silanes - chemistry ; Silanes - pharmacology ; staphylococcus-aureus ; Streptococcus sanguinis ; Surface Properties ; Titani ; Titanium ; Titanium - chemistry ; Titanium - pharmacology ; transfer radical polymerization ; Àrees temàtiques de la UPC</subject><ispartof>Biomacromolecules, 2015-02, Vol.16 (2), p.483-496</ispartof><rights>Copyright © 2014 American Chemical Society</rights><rights>info:eu-repo/semantics/openAccess <a href="http://creativecommons.org/licenses/by-nc-nd/3.0/es/">http://creativecommons.org/licenses/by-nc-nd/3.0/es/</a></rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a491t-1577e0f3f0e05ba18ded39bf48be54ff565b0cbb62df900e4e80ea45417d09eb3</citedby><cites>FETCH-LOGICAL-a491t-1577e0f3f0e05ba18ded39bf48be54ff565b0cbb62df900e4e80ea45417d09eb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bm501528x$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bm501528x$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,780,784,885,2765,26974,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25545728$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Godoy-Gallardo, Maria</creatorcontrib><creatorcontrib>Mas-Moruno, Carlos</creatorcontrib><creatorcontrib>Yu, Kai</creatorcontrib><creatorcontrib>Manero, José M</creatorcontrib><creatorcontrib>Gil, Francisco J</creatorcontrib><creatorcontrib>Kizhakkedathu, Jayachandran N</creatorcontrib><creatorcontrib>Rodriguez, Daniel</creatorcontrib><title>Antibacterial Properties of hLf1–11 Peptide onto Titanium Surfaces: A Comparison Study Between Silanization and Surface Initiated Polymerization</title><title>Biomacromolecules</title><addtitle>Biomacromolecules</addtitle><description>Dental implant failure can be associated with infections that develop into peri-implantitis. In order to reduce biofilm formation, several strategies focusing on the use of antimicrobial peptides (AMPs) have been studied. To covalently immobilize these molecules onto metallic substrates, several techniques have been developed, including silanization and polymer brush prepared by surface-initiated atom transfer radical polymerization (ATRP), with varied peptide binding yield and antibacterial performance. The aim of the present study was to compare the efficiency of these methods to immobilize the lactoferrin-derived hLf1–11 antibacterial peptide onto titanium, and evaluate their antibacterial activity in vitro. Smooth titanium samples were coated with hLf1–11 peptide under three different conditions: silanization with 3-aminopropyltriethoxysilane (APTES), and polymer brush based coatings with two different silanes. Peptide presence was determined by X-ray photoelectron spectroscopy, and the mechanical stability of the coatings was studied under ultrasonication. The LDH assays confirmed that HFFs viability and proliferation were no affected by the treatments. The in vitro antibacterial properties of the modified surfaces were tested with two oral strains (Streptococcus sanguinis and Lactobacillus salivarius) showing an outstanding reduction. A higher decrease in bacterial attachment was noticed when samples were modified by ATRP methods compared to silanization. This effect is likely due to the capacity to immobilize more peptide on the surfaces using polymer brushes and the nonfouling nature of polymer PDMA segment.</description><subject>Anti-Bacterial Agents - chemistry</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>antimicrobial peptides</subject><subject>attachment</subject><subject>brushes</subject><subject>Cell Survival - drug effects</subject><subject>Cell Survival - physiology</subject><subject>cell-adhesive</subject><subject>Cells, Cultured</subject><subject>Dental Implants</subject><subject>Enginyeria dels materials</subject><subject>escherichia-coli</subject><subject>Humans</subject><subject>Implants artificials</subject><subject>in-vitro</subject><subject>Lactobacillus salivarius</subject><subject>lactoferricin-b</subject><subject>Lactoferrin - chemistry</subject><subject>Lactoferrin - pharmacology</subject><subject>Male</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - pharmacology</subject><subject>Polymerization</subject><subject>roughness</subject><subject>Silanes - chemistry</subject><subject>Silanes - pharmacology</subject><subject>staphylococcus-aureus</subject><subject>Streptococcus sanguinis</subject><subject>Surface Properties</subject><subject>Titani</subject><subject>Titanium</subject><subject>Titanium - chemistry</subject><subject>Titanium - pharmacology</subject><subject>transfer radical polymerization</subject><subject>Àrees temàtiques de la UPC</subject><issn>1525-7797</issn><issn>1526-4602</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>XX2</sourceid><recordid>eNqNkc9u1DAQxiMEon_gwAsgX5DoIWXs2HHCbVkBrbQSK7WcLTsZC1dJHGxHsJx4BnhDngSX3ZYLBw7WeOTf92k8X1E8o3BOgdFXZhRABWu-PiiOc61LXgN7-OcuSilbeVScxHgDAG3FxePiiAnBhWTNcfFjNSVndJcwOD2QbfAzhuQwEm_Jp42lv77_pJRscU6uR-Kn5Mm1S3pyy0iulmB1h_E1WZG1H2cdXPQTuUpLvyNvMH1BzJ0bMv1NJ5ef9NTfqcjl5JLTCXuy9cNuzAPsoSfFI6uHiE8P9bT4-O7t9fqi3Hx4f7lebUrNW5pKKqREsJUFBGE0bXrsq9ZY3hgU3FpRCwOdMTXrbQuAHBtAzQWnsocWTXVa0L1vF5dOBewwdDopr93f5vYwkEyxrGtk1rzca-bgPy8Ykxpd7HDIX0S_REXrGnjecwX_gYqKVpRSltGzwyTBxxjQqjm4UYedoqBuE1b3CWf2-cF2MSP29-RdpBl4sQd0F9WNX8KUl_gPo99Iia9-</recordid><startdate>20150209</startdate><enddate>20150209</enddate><creator>Godoy-Gallardo, Maria</creator><creator>Mas-Moruno, Carlos</creator><creator>Yu, Kai</creator><creator>Manero, José M</creator><creator>Gil, Francisco J</creator><creator>Kizhakkedathu, Jayachandran N</creator><creator>Rodriguez, Daniel</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>XX2</scope></search><sort><creationdate>20150209</creationdate><title>Antibacterial Properties of hLf1–11 Peptide onto Titanium Surfaces: A Comparison Study Between Silanization and Surface Initiated Polymerization</title><author>Godoy-Gallardo, Maria ; Mas-Moruno, Carlos ; Yu, Kai ; Manero, José M ; Gil, Francisco J ; Kizhakkedathu, Jayachandran N ; Rodriguez, Daniel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a491t-1577e0f3f0e05ba18ded39bf48be54ff565b0cbb62df900e4e80ea45417d09eb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Anti-Bacterial Agents - chemistry</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>antimicrobial peptides</topic><topic>attachment</topic><topic>brushes</topic><topic>Cell Survival - drug effects</topic><topic>Cell Survival - physiology</topic><topic>cell-adhesive</topic><topic>Cells, Cultured</topic><topic>Dental Implants</topic><topic>Enginyeria dels materials</topic><topic>escherichia-coli</topic><topic>Humans</topic><topic>Implants artificials</topic><topic>in-vitro</topic><topic>Lactobacillus salivarius</topic><topic>lactoferricin-b</topic><topic>Lactoferrin - chemistry</topic><topic>Lactoferrin - pharmacology</topic><topic>Male</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - pharmacology</topic><topic>Polymerization</topic><topic>roughness</topic><topic>Silanes - chemistry</topic><topic>Silanes - pharmacology</topic><topic>staphylococcus-aureus</topic><topic>Streptococcus sanguinis</topic><topic>Surface Properties</topic><topic>Titani</topic><topic>Titanium</topic><topic>Titanium - chemistry</topic><topic>Titanium - pharmacology</topic><topic>transfer radical polymerization</topic><topic>Àrees temàtiques de la UPC</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Godoy-Gallardo, Maria</creatorcontrib><creatorcontrib>Mas-Moruno, Carlos</creatorcontrib><creatorcontrib>Yu, Kai</creatorcontrib><creatorcontrib>Manero, José M</creatorcontrib><creatorcontrib>Gil, Francisco J</creatorcontrib><creatorcontrib>Kizhakkedathu, Jayachandran N</creatorcontrib><creatorcontrib>Rodriguez, Daniel</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Recercat</collection><jtitle>Biomacromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Godoy-Gallardo, Maria</au><au>Mas-Moruno, Carlos</au><au>Yu, Kai</au><au>Manero, José M</au><au>Gil, Francisco J</au><au>Kizhakkedathu, Jayachandran N</au><au>Rodriguez, Daniel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Antibacterial Properties of hLf1–11 Peptide onto Titanium Surfaces: A Comparison Study Between Silanization and Surface Initiated Polymerization</atitle><jtitle>Biomacromolecules</jtitle><addtitle>Biomacromolecules</addtitle><date>2015-02-09</date><risdate>2015</risdate><volume>16</volume><issue>2</issue><spage>483</spage><epage>496</epage><pages>483-496</pages><issn>1525-7797</issn><eissn>1526-4602</eissn><abstract>Dental implant failure can be associated with infections that develop into peri-implantitis. In order to reduce biofilm formation, several strategies focusing on the use of antimicrobial peptides (AMPs) have been studied. To covalently immobilize these molecules onto metallic substrates, several techniques have been developed, including silanization and polymer brush prepared by surface-initiated atom transfer radical polymerization (ATRP), with varied peptide binding yield and antibacterial performance. The aim of the present study was to compare the efficiency of these methods to immobilize the lactoferrin-derived hLf1–11 antibacterial peptide onto titanium, and evaluate their antibacterial activity in vitro. Smooth titanium samples were coated with hLf1–11 peptide under three different conditions: silanization with 3-aminopropyltriethoxysilane (APTES), and polymer brush based coatings with two different silanes. Peptide presence was determined by X-ray photoelectron spectroscopy, and the mechanical stability of the coatings was studied under ultrasonication. The LDH assays confirmed that HFFs viability and proliferation were no affected by the treatments. The in vitro antibacterial properties of the modified surfaces were tested with two oral strains (Streptococcus sanguinis and Lactobacillus salivarius) showing an outstanding reduction. A higher decrease in bacterial attachment was noticed when samples were modified by ATRP methods compared to silanization. This effect is likely due to the capacity to immobilize more peptide on the surfaces using polymer brushes and the nonfouling nature of polymer PDMA segment.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>25545728</pmid><doi>10.1021/bm501528x</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - pharmacology antimicrobial peptides attachment brushes Cell Survival - drug effects Cell Survival - physiology cell-adhesive Cells, Cultured Dental Implants Enginyeria dels materials escherichia-coli Humans Implants artificials in-vitro Lactobacillus salivarius lactoferricin-b Lactoferrin - chemistry Lactoferrin - pharmacology Male Peptide Fragments - chemistry Peptide Fragments - pharmacology Polymerization roughness Silanes - chemistry Silanes - pharmacology staphylococcus-aureus Streptococcus sanguinis Surface Properties Titani Titanium Titanium - chemistry Titanium - pharmacology transfer radical polymerization Àrees temàtiques de la UPC |
title | Antibacterial Properties of hLf1–11 Peptide onto Titanium Surfaces: A Comparison Study Between Silanization and Surface Initiated Polymerization |
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