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231225s2020 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.0c01790
|2 doi
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|a pubmed24n1046.xml
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|a (NLM)32830498
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|a DE-627
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|e rakwb
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|a eng
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|a Beyer, Cindy D
|e verfasserin
|4 aut
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|a Low Fouling Peptides with an All (d) Amino Acid Sequence Provide Enhanced Stability against Proteolytic Degradation While Maintaining Low Antifouling Properties
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|c 2020
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 15.10.2020
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|a Date Revised 15.10.2020
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|a published: Print-Electronic
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|a Citation Status PubMed-not-MEDLINE
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|a 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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|a Journal Article
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a Reback, Matthew L
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Heinen, Natalie
|e verfasserin
|4 aut
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|a Thavalingam, Sugina
|e verfasserin
|4 aut
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|a Rosenhahn, Axel
|e verfasserin
|4 aut
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|a Metzler-Nolte, Nils
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 36(2020), 37 vom: 22. Sept., Seite 10996-11004
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
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|g volume:36
|g year:2020
|g number:37
|g day:22
|g month:09
|g pages:10996-11004
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|u http://dx.doi.org/10.1021/acs.langmuir.0c01790
|3 Volltext
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