| Title: | Resistance of Zwitterionic Peptide Monolayers to Biofouling |
| Author(s): | Ederth T; Lerm M; Orihuela B; Rittschof D; |
| Address: | "Division of Molecular Physics, Department of Physics, Chemistry and Biology , Linkoping University , SE-581 83 Linkoping , Sweden. Division of Microbiology and Molecular Medicine, Department of Clinical and Experimental Medicine , Linkoping University , SE-581 83 Linkoping , Sweden. Duke University Marine Laboratory, Nicholas School of the Environment, Duke University , Beaufort , North Carolina 28516-9721 , United States" |
| DOI: | 10.1021/acs.langmuir.8b01625 |
| ISSN/ISBN: | 1520-5827 (Electronic) 0743-7463 (Linking) |
| Abstract: | "Self-assembled monolayers (SAMs) are widely used in science and engineering, and recent progress has demonstrated the utility of zwitterionic peptides with alternating lysine (K) and glutamic acid (E) residues for antifouling purposes. Aiming at developing a peptide-based fouling-resistant SAM suitable for presentation of surface-attached pheromones for barnacle larvae, we have investigated five different peptide SAMs, where four are based on the EK motif, and the fifth was designed based on general principles for fouling resistance. The SAMs were formed by self-assembly onto gold substrates via cysteine residues on the peptides, and formation of SAMs was verified via ellipsometry, wettability, infrared reflection-absorption spectroscopy and cyclic voltammetry. Settlement of cypris larvae of the barnacle Balanus (=Amphibalanus) amphitrite, the target of pheromone studies, was tested. SAMs were also subjected to fouling assays using protein solutions, blood serum, and the bacterium Mycobacterium marinum. The results confirm the favorable antifouling properties of EK-containing peptides in most of the assays, although this did not apply to the barnacle larvae settlement test, where settlement was low on only one of the peptide SAMs. The one peptide that had antifouling properties for barnacles did not contain a pheromone motif, and would not be susceptible to degredation by common serine proteases. We conclude that the otherwise broadly effective antifouling properties of EK-containing peptide SAMs is not directly applicable to barnacles, and that great care must be exercised in the design of peptide-based SAMs for presentation of barnacle-specific ligands" |
| Keywords: | "Adsorption/drug effects Amino Acid Sequence Animals Biofouling/*prevention & control Blood Gold/chemistry Humans *Membranes, Artificial Mycobacterium marinum/metabolism Peptides/*chemistry Proteins/chemistry Surface Properties Thoracica/metabolism;" |
| Notes: | "MedlineEderth, Thomas Lerm, Maria Orihuela, Beatriz Rittschof, Daniel eng Research Support, Non-U.S. Gov't 2018/08/15 Langmuir. 2019 Feb 5; 35(5):1818-1827. doi: 10.1021/acs.langmuir.8b01625. Epub 2018 Aug 28" |
