Enzymatic assembly of adhesive molecular networks with sequence-dependent mechanical properties inspired by mussel foot proteins
Literature Information
Publication Date
2019-01-14
DOI
10.1039/C8PY01581C
Impact Factor
5.582
Authors
Byung Min Park, Jiren Luo
View Original
Abstract
By inserting short peptide motifs derived from Mfp-3 and Mfp-5 into elastin-like polypeptides (ELPs), we created several recombinant protein polymers that can form adhesive hydrogels upon enzymatic oxidation. The resulting materials exhibited sequence-dependent bulk mechanical properties and strong adhesiveness. The materials also showed excellent cytocompatibility toward encapsulated human alveolar epithelial cells. This study illustrates a new strategy for designing adhesive materials for biomedical and research purposes.
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Source Journal
Polymer Chemistry
CiteScore:
8.6
Self-citation Rate:
7.3%
Articles per Year:
457
Polymer Chemistry welcomes submissions in all areas of polymer science that have a strong focus on macromolecular chemistry. Manuscripts may cover a broad range of fields, yet no direct application focus is required.
Recommended Compounds
1-Methyl-3-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)-1H-pyrazole
CAS Number:
1020174-04-2
Molecular Formula:
C10H17BN2O2
![[4-(Heptyloxy)phenyl]boronic acid structure](https://static.chemtradehub.com/structs/136/136370-19-9-ad33.webp "[4-(Heptyloxy)phenyl]boronic acid structure")
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