1. Low Fouling Peptides with an All (<scp>d</scp>) Amino Acid Sequence Provide Enhanced Stability against Proteolytic Degradation While Maintaining Low Antifouling Properties
- Author
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Axel Rosenhahn, Natalie Heinen, Sugina Thavalingam, Nils Metzler-Nolte, Cindy D. Beyer, and Matthew L. Reback
- Subjects
chemistry.chemical_classification ,biology ,Fouling ,Chemistry ,Cobetia marina ,Sequence (biology) ,02 engineering and technology ,Surfaces and Interfaces ,010402 general chemistry ,021001 nanoscience & nanotechnology ,Condensed Matter Physics ,biology.organism_classification ,01 natural sciences ,0104 chemical sciences ,Amino acid ,Biofouling ,chemistry.chemical_compound ,Marine bacteriophage ,Adsorption ,Electrochemistry ,Biophysics ,General Materials Science ,Lysozyme ,0210 nano-technology ,Spectroscopy - Abstract
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.
- Published
- 2020
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