Chemically Immobilized Antimicrobial Peptide on Polymer and Self-Assembled Monolayer Substrates

Abstract

Surfaces with chemically immobilized antimicrobial peptides have been shown to have great potential in various applications such as biosensors and antimicrobial coatings. This research investigated the chemical immobilization of a cecropin-melittin hybrid antimicrobial peptide on two different surfaces, a polymer surface prepared by chemical vapor deposition (CVD) polymerization and a self-assembled monolayer surface. We probed the structure of immobilized peptides using spectroscopic methods and correlated such structural information to the measured antimicrobial activity. We found that the hybrid peptide adopts an α-helical structure after immobilization onto both surfaces. As we have shown previously for another α-helical peptide, MSI-78, immobilized on a SAM, we found that the α-helical hybrid peptide lies down when it contacts bacteria. This study shows that the antimicrobial activity of the surface-immobilized peptides on the two substrates can be well explained by the spectroscopically measured peptide structural data. In addition, it was found that the polymer-based antimicrobial peptide coating is more stable. This is likely due to the fact that the SAM prepared using silane may be degraded after several days whereas the polymer prepared by CVD polymerization is more stable than the SAM, leading to a more stable antimicrobial coating.

Surface Design for Immobilization of an Antimicrobial Peptide Mimic for Efficient Anti‐Biofouling

“…One such peptoid has also been synthesized as part of a surface grafted peptoid brush but a high level of overall bacterial attachment was observed . Natural AMPs such as hLf1‐11, LL‐37, and melamine have also been immobilized with varying results . These studies apply bioconjugation techniques such as maleimide‐thiol, amide, and alkyne–azide „click“ coupling to enable covalent surface immobilization.…”

Functionalization of hydrophobic surfaces with antimicrobial peptides immobilized on a bio-interfactant layer

“…[18][19][20] This method may be applied on hydrophobic polymer surfaces aer applying a process to increase the concentration of functional groups such as hydroxyl and carbonyl groups, and next covalent attachment using click chemistry. 21 Another viable method is solid phase peptide synthesis on polymer resins in which the protected amino acids are incorporated by assembling the peptide sequence from its C-to its N-terminus; however, these methods are time consuming and costly. [21][22][23] Although peptides with hydrophobic amino acids may adsorb strongly enough on hydrophobic surfaces to form a stable lm under controlled conditions.…”

“…21 Another viable method is solid phase peptide synthesis on polymer resins in which the protected amino acids are incorporated by assembling the peptide sequence from its C-to its N-terminus; however, these methods are time consuming and costly. [21][22][23] Although peptides with hydrophobic amino acids may adsorb strongly enough on hydrophobic surfaces to form a stable lm under controlled conditions. The peptides when are amphiphilic likely adsorb with their hydrophobic segments facing hydrophobic surfaces and the restricted orientation of the peptide might cause a reduction in its antimicrobial properties.…”

Defensin-Like Peptides and Their Antimicrobial Activity in Free-Form and Immobilized on Material Surfaces

“…A polymer surface (i.e., dibromomaleimide polymer substrate) prepared by chemical vapour deposition (CVD) and functionalized with AMPs showed a better antimicrobial stability when compared to a self-assembled monolayer (SAM). When exposed to air, this polymer showed slower detachment of bound AMPs when compared to SAM [95]. Additionally, orientation of AMPs was also retained.…”