Covalent immobilization of hLf1-11 peptide on a titanium surface reduces bacterial adhesion and biofilm formation

Maria Godoy Gallardo, Carlos Mas-Moruno, Maria C. Fernandez-Calderon, Ciro Perez-Giraldo, Jose M. Manero, Fernando Albericio, Francisco J. Gil, Daniel Rodriguez

Research output: Contribution to journalJournal articleResearchpeer-review


Bacterial infection represents a major cause of implant failure in dentistry. A common approach to overcoming this issue and treating pen-implant infection consists in the use of antibiotics. However, the rise of multidrug-resistant bacteria poses serious concerns to this strategy. A promising alternative is the use of antimicrobial peptides due to their broad-spectrum activity against bacteria and reduced bacterial resistance responses. The aim of the present study was to determine the in vitro antibacterial activity of the human lactoferrin-derived peptide hLf1-11 anchored to titanium surfaces. To this end, titanium samples were functionalized with the hLf1-11 peptide either by silanization methods or physical adsorption. X-ray photoelectron spectroscopy analyses confirmed the successful covalent attachment of the hLf1-11 peptide onto titanium surfaces. Lactate dehydrogenase assay determined that hLf1-11 peptide did not affect fibroblast viability. An outstanding reduction in the adhesion and early stages of biofilm formation of Streptococcus sanguinis and Lactobacillus salivarius was observed on the biofunctionalized surfaces compared to control non-treated samples. Furthermore, samples coated with the hLf1-11 peptide inhibited the early stages of bacterial growth. Thus, this strategy holds great potential to develop antimicrobial biomaterials for dental applications. (C) 2014 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.
Original languageEnglish
JournalActa Biomaterialia
Issue number8
Pages (from-to)3522-3534
Publication statusPublished - 2014
Externally publishedYes


  • Titanium
  • Lactoferrin peptide
  • Biofunctionalization
  • Bacterial adhesion
  • Antimicrobial peptide
  • Biomaterials
  • Biomedical Engineering
  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Medicine (all)
  • human lactoferrin 1-11
  • lactate dehydrogenase
  • lactoferrin
  • polypeptide antibiotic agent
  • titanium
  • unclassified drug
  • antiinfective agent
  • biomaterial
  • lactoferrin (1-11), human
  • peptide fragment
  • protein binding
  • adsorption
  • antibacterial activity
  • article
  • bacterial growth
  • bacterium adherence
  • biofilm
  • cell viability
  • contact angle
  • controlled study
  • covalent bond
  • enzyme assay
  • fibroblast
  • growth inhibition
  • human
  • human cell
  • in vitro study
  • Lactobacillus salivarius
  • morphology
  • nonhuman
  • plankton
  • priority journal
  • protein immobilization
  • Streptococcus sanguinis
  • surface property
  • X ray photoelectron spectroscopy
  • cell survival
  • chemistry
  • drug effects
  • growth, development and aging
  • materials testing
  • physiology
  • synthesis
  • Bacteria (microorganisms)
  • Adsorption
  • Anti-Infective Agents
  • Bacterial Adhesion
  • Biofilms
  • Cell Survival
  • Coated Materials, Biocompatible
  • Lactoferrin
  • Materials Testing
  • Peptide Fragments
  • Protein Binding
  • Surface Properties

Cite this

Gallardo, M. G., Mas-Moruno, C., Fernandez-Calderon, M. C., Perez-Giraldo, C., Manero, J. M., Albericio, F., Gil, F. J., & Rodriguez, D. (2014). Covalent immobilization of hLf1-11 peptide on a titanium surface reduces bacterial adhesion and biofilm formation. Acta Biomaterialia, 10(8), 3522-3534.