Abstract
Biofunctional scaffolds for the delivery of living cells are of the utmost importance for regenerative medicine. Herein, a novel, robust “spiraled horn” scaffold was elucidated through the Co2+-promoted hierarchical assembly of two collagen mimetic peptides, NCoH and HisCol. Each “horn” displayed a periodic banding pattern with band lengths corresponding to the length of the collagen peptide triple helix. Strand exchange between the two peptide trimers resulted in failure to form this intricate morphology, lending support to a precise metal-ligand-based mechanism of assembly. Little change occurred to the observed morphology when the Co2+ concentration was varied from 0.5 to 4.0 mM, and the scaffold was found to be fully formed within two minutes of exposure to the metal ion. The horned network also displayed biological functionality by binding to a His-tagged fluorophore and associating with cells.
Highlights
Collagen is a crucial component of the extracellular matrix, supporting the growth and development of cells [1]
A more practical and cost-effective alternative is the use of collagen mimetic peptides (CMPs), designed with specific sequences to promote self-assembly through native chemical ligation [9], cationic-π interactions [10], cysteine bridge formation [11,12], electrostatic interactions [13,14], hydrophobic packing [15,16], and metal-ligand interactions [17], the latter of which is described in more detail below
We have shown that the Co2+-promoted assembly of two collagen mimetic peptides, NCoH and
Summary
Collagen is a crucial component of the extracellular matrix, supporting the growth and development of cells [1]. A more practical and cost-effective alternative is the use of collagen mimetic peptides (CMPs), designed with specific sequences to promote self-assembly through native chemical ligation [9], cationic-π interactions [10], cysteine bridge formation [11,12], electrostatic interactions [13,14], hydrophobic packing [15,16], and metal-ligand interactions [17], the latter of which is described in more detail below. Still other studies made use of a “sticky-ended” nucleation strategy, inspired by the assembly of DNA and coiled-coiled helices, in which staggered collagen helices, generated through the exploitation of lysine-aspartate axial salt bridges, were pieced together into microfibers [19]. Few strategies have proven to be as elegant and as versatile as metal-promoted self-assembly
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