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. 2019 Mar 18;4(1):25. doi: 10.3390/biomimetics4010025

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Metal coordinating coiled coil (CC) cross-linked hydrogel. (A) Sequences of the acidic (A_4H3) and basic (B_4H3) CC-forming peptides, carrying three histidines (bold) in the solvent-exposed f positions. Cysteine residues were added at the N-terminus of A_4H3 and the C-terminus of B_4H3 to facilitate coupling to maleimide-functionalized star-shaped poly(ethylene glycol) (star-PEG–maleimide). (B) Structure of the CC constructed in CCBuilder 2.0 [29]. The side chains of the histidine residues are highlighted. (C) Schematic representation of the hydrogel preparation and structure. A_4H3 and B_4H3 are separately coupled to star-PEG–maleimide via their terminal cysteine residues. The resulting PEG–peptide conjugates are then mixed in a 1:1 ratio to obtain a CC cross-linked hydrogel.