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Engineering Complementary Hydrophobic Interactions to Control β‑Hairpin Peptide Self-Assembly, Network Branching, and Hydrogel Properties
The MAX1 β-hairpin peptide (VKVKVKVK-V(D)PPT-KVKVKVKV-NH(2)) has been shown to form nanofibrils having a cross-section of two folded peptides forming a hydrophobic, valine-rich core, and the polymerized fibril exhibits primarily β-sheet hydrogen bonding.(1–7) These nanofibrils form hydrogel networks...
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| 出版年: | Biomacromolecules |
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| 主要な著者: | , , , , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
2014
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7720678/ https://ncbi.nlm.nih.gov/pubmed/25251904 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bm500874t |
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