Low Fouling Peptides with an All (d) Amino Acid Sequence Provide Enhanced Stability against Proteolytic Degradation while Maintaining Low Antifouling Properties

Beyer, C.D. and Reback, M.L. and Heinen, N. and Thavalingam, S. and Rosenhahn, A. and Metzler-Nolte, N.

Volume: 36 Pages: 10996-11004
DOI: 10.1021/acs.langmuir.0c01790
Published: 2020

Peptide-functionalized surfaces, composed of optimized l-peptides, show a high resistance toward nonspecific adsorption of proteins. As l-peptides are known to be prone to proteolytic degradation, the aim of this work is to enhance the stability against enzymatic degradation by using the all d-peptide mirror image of the optimized l-peptides and to determine if the all d-enantiomer retains the protein-resistant and antifouling properties. Two l-peptides and their d-peptide mirror images, some of them containing the nonproteinogenic amino acid α-aminoisobutyric acid (Aib), were synthesized and tested against non-specific adsorption of the proteins lysozyme and fibrinogen and the settlement of marine diatom Navicula perminuta and marine bacteria Cobetia marina. Both the d-enantiomer and the insertion of Aib protected the peptides from proteolytic degradation. Protein resistance was enhanced with the d-enantiomers while maintaining the resistance toward diatoms. Copyright © 2020 American Chemical Society.

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