title: Temporin-SHa peptides grafted on gold surfaces display antibacterial activity.
abstract: Development of resistant bacteria onto biomaterials is a major problem leading to nosocomial infections. Antimicrobial peptides are good candidates for the generation of antimicrobial surfaces because of their broad-spectrum activity and their original mechanism of action (i.e. rapid lysis of the bacterial membrane) making them less susceptible to the development of bacterial resistance. In this study, we report on the covalent immobilisation of temporin-SHa on a gold surface modified by a thiolated self-assembled monolayer. Temporin-SHa (FLSGIVGMLGKLF amide) is a small hydrophobic and low cationic antimicrobial peptide with potent and very broad-spectrum activity against Gram-positive and Gram-negative bacteria, yeasts and parasites. We have analysed the influence of the binding mode of temporin-SHa on the antibacterial efficiency by using a covalent binding either via the peptide NH2 groups (random grafting of α- and ε-NH2 to the surface) or via its C-terminal end (oriented grafting using the analogue temporin-SHa-COOH). The surface functionalization was characterised by IR spectroscopy (polarisation modulation reflection absorption IR spectroscopy) while antibacterial activity against Listeria ivanovii was assessed by microscopy techniques, such as atomic force microscopy and scanning electron microscopy equipped with a field emission gun. Our results revealed that temporin-SHa retains its antimicrobial activity after covalent grafting. A higher amount of bound temporin-SHa is observed for the C-terminally oriented grafting compared with the random grafting (NH2 groups). Temporin-SHa therefore represents an attractive candidate as antimicrobial coating agent.
authors.affiliation: Sorbonne Universités, UPMC Univ Paris 06, UMR 7197, Laboratoire de Réactivité de Surface (LRS), F-75005, Paris, France; CNRS, UMR 7197, Laboratoire de Réactivité de Surface, F-75005, Paris, France.
authors.forename: Andres
authors.initials: A
authors.lastname: Lombana
authors.forename: Zahid
authors.initials: Z
authors.lastname: Raja
authors.forename: Sandra
authors.initials: S
authors.lastname: Casale
authors.forename: Claire-Marie
authors.initials: CM
authors.lastname: Pradier
authors.forename: Thierry
authors.initials: T
authors.lastname: Foulon
authors.forename: Ali
authors.initials: A
authors.lastname: Ladram
authors.forename: Vincent
authors.initials: V
authors.lastname: Humblot
mesh_terms: D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000494:pharmacology; D020099:Coated Materials, Biocompatible / Q000737:chemistry / Q000494:pharmacology; D006046:Gold / Q000737:chemistry*; D008087:Listeria / Q000187:drug effects; D008826:Microbial Sensitivity Tests; D018625:Microscopy, Atomic Force; D008855:Microscopy, Electron, Scanning; D013499:Surface Properties
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D020099:Coated Materials, Biocompatible; C000595450:temporin-SHa peptide, Pelophylax saharica; D006046:Gold
keywords: antimicrobial peptide; atomic force microscopy; scanning electron microscopy; surface functionalisation; temporin-SHa