| Autor: |
Pranothi Mulinti, Dorina Diekjürgen, Kristen Kurtzeborn, Narayanaganesh Balasubramanian, Shane J. Stafslien, David W. Grainger, Amanda E. Brooks |
| Jazyk: |
angličtina |
| Rok vydání: |
2022 |
| Předmět: |
|
| Zdroj: |
Bioengineering, Vol 9, Iss 2, p 46 (2022) |
| Druh dokumentu: |
article |
| ISSN: |
2306-5354 |
| DOI: |
10.3390/bioengineering9020046 |
| Popis: |
Governed by established structure–property relationships, peptide motifs comprising major ampullate spider silk confer a balance of strength and extensibility. Other biologically inspired small peptide motifs correlated to specific functionalities can be combined within these units to create designer silk materials with new hybrid properties. In this study, a small basic peptide, (ARKKAAKA) known to both bind heparin and mimic an antimicrobial peptide, was genetically linked to a protease-resistant, mechanically robust silk-like peptide, MaSp2. Purified fusion proteins (four silk domains and four heparin-binding peptide repeats) were expressed in E. coli. Successful fusion of a MaSp2 spider silk peptide with the heparin-binding motif was shown using a variety of analytical assays. The ability of the fusion peptide to bind heparin was assessed with ELISA and was further tested for its anticoagulant property using aPTT assay. Its intrinsic property to inhibit bacterial growth was evaluated using zone of inhibition and crystal violet (CV) assays. Using this strategy, we were able to link the two types of genetic motifs to create a designer silk-like protein with improved hemocompatibility and antimicrobial properties. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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