Low Fouling Peptides with an All (d) Amino Acid Sequence Provide Enhanced Stability against Proteolytic Degradation While Maintaining Low Antifouling Properties
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-pepti...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 36(2020), 37 vom: 22. Sept., Seite 10996-11004 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2020
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, U.S. Gov't, Non-P.H.S. |
| Zusammenfassung: | 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 |
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| Beschreibung: | Date Completed 15.10.2020 Date Revised 15.10.2020 published: Print-Electronic Citation Status PubMed-not-MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/acs.langmuir.0c01790 |