Rational Design of Amphiphilic Peptides and Its Effect on Antifouling Performance

Abstract

Biofouling, the unwanted adhesion of organisms to surfaces, has a negative impact on energy, food, water, and health resources. One possible strategy to fight biofouling is to modify the surface using a peptide-based coating that will change the surface properties. We reveal the importance of rational design and positioning of individual amino acids in an amphiphilic peptide sequence. By just manipulating the position of the amino acids within the peptide chain having the same chemical composition, we improved the antifouling performance of an amphiphilic peptide-based coating, Phe(4-F)-Lys-DOPA, by 30%. We have judiciously tailored the peptide configurations to achieve the best antifouling performance by (i) positioning the amino acid lysine adjacent to the DOPA moiety in the linear peptide chain for better adhesion, (ii) having a linear fluorinated N-terminal to improve the packing density of the film by straightening the peptide chain, and (iii) placing DOPA at the C-terminal. We have also compared the antifouling performances of amphiphilic, hydrophobic, hydrophilic, and alternately arranged peptides. Our results show a reduction of ∼80% in bacterial adhesion for an amphiphilic peptide-coated surface when compared to a bare titanium surface. This work provides important strategic design guidelines for future peptide-related materials that have effective antifouling properties.

Biocompatible Lipopeptide-Based Antibacterial Hydrogel

“…These make them promising biomaterials for different purposes with versatile applications. Lysine and arginine amino acids possess positive charge in their side chains, which are often incorporated in different peptides and polymers to generate or enhance antibacterial properties. − The negatively charged membrane often interacts with cationic biomaterials through electrostatic interactions followed by attachment of the hydrophobic counter parts into the lipid layer of the membrane. This could lead to the formation of pores in the bacterial cell membrane, thereby killing the bacteria.…”

Amphiphilic Peptide with Dual Functionality Resists Biofouling

“…The peptide comprises two sets of five l -lysine residues and two sets of five 4-fluoro- l -phenylalanine residues (20 amino acids in total, Scheme a). We used fluorinated phenylalanine residues since we assumed, based on our previous research, that these amino acids will provide the peptide with antifouling properties. , The number of lysine in each set of amino acids is five as it is shown that the antimicrobial activity of cationic amino acids is maximal when the charge is +5 . To attach the peptide to the surface, we used the amino acid l -DOPA.…”

Surface Modification by Nano-Structures Reduces Viable Bacterial Biofilm in Aerobic and Anaerobic Environments

“…Depending on the specific building blocks and the assembly conditions, various nano-structured morphologies, including fibrils, tubes, sheets, tapes, spheres, vesicles and hydrogel matrices, can be formed in vitro, allowing for distinctive functional possibilities [ 28 , 30 , 31 , 32 , 33 , 34 , 35 ], mainly in tissue engineering [ 36 , 37 , 38 , 39 ], regenerative medicine [ 40 ], cell culture [ 41 , 42 , 43 , 44 ], drug delivery [ 36 , 39 , 45 , 46 , 47 , 48 , 49 ], bio-imaging [ 50 , 51 ] and fabric functionalization [ 52 ]. Coatings based on self-assembled peptides, primarily for antibacterial purposes, have been recently reported [ 5 , 12 , 13 , 21 , 53 , 54 , 55 , 56 ]. The self-assembly of the tri-peptide DOPA-Phe(4F)-Phe(4F)-OMe into an antifouling coating by the dip-coating technique was reported [ 13 ].…”