Mechanical properties of a self-assembling oligopeptide matrix

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Abstract
We have begun studies of a novel type of biomaterial derived from a recently-discovered class of ionic self-complementary oligopeptides. These short peptides (typically 8, 16, 24, or 32 amino acid residues with internally-repeating sequences) self-assemble in aqueous salt solution into three-dimensional matrices capable of favorable interactions with cells, and offer promise for useful bioengineering design based on rational changes in sequence. In this paper we present preliminary results on mechanical properties, combining experimental and theoretical approaches, of one particular example of these peptide materials, EFK8. The static elastic modulus was measured using an apparatus designed to allow sample fabrication and mechanical testing in the same system with the sample in aqueous solution. The material microstructure was examined by SEM and the measurements interpreted with the aid of a model for cellular solids. Values for the elastic modulus increased from 1.59 ± 0.06 to 14.7 ± 1.0 kPa for peptide concentrations increasing from 2.7 to 10 mg ml-1. SEM photographs showed the microstructure to consist of a relatively homogeneous lattice with fiber thickness of 10 - 30 nm independent of peptide concentration, but with fiber density increasing with peptide concentration. This behavior is consistent with scaling predictions from the cellular solids model and yields an estimate for the individual fiber elastic modulus in the range of 1-20 MPa. We therefore have provided some initial physical principles for guiding improvement of the mechanical properties of these new materials.