Towards Developing Bioresponsive, Self-Assembled Peptide Materials: Dynamic Morphology and Fractal Nature of Nanostructured Matrices

Materials
K M Koss, Larry D Unsworth

Abstract

(Arginine-alanine-aspartic acid-alanine)₄ ((RADA)₄) nanoscaffolds are excellent candidates for use as peptide delivery vehicles: they are relatively easy to synthesize with custom bio-functionality, and assemble in situ to allow a focal point of release. This enables (RADA)₄ to be utilized in multiple release strategies by embedding a variety of bioactive molecules in an all-in-one "construct". One novel strategy focuses on the local, on-demand release of peptides triggered via proteolysis of tethered peptide sequences. However, the spatial-temporal morphology of self-assembling nanoscaffolds may greatly influence the ability of enzymes to both diffuse into as well as actively cleave substrates. Fine structure and its impact on the overall effect on peptide release is poorly understood. In addition, fractal networks observed in nanoscaffolds are linked to the fractal nature of diffusion in these systems. Therefore, matrix morphology and fractal dimension of virgin (RADA)₄ and mixtures of (RADA)₄ and matrix metalloproteinase 2 (MMP-2) cleavable substrate modified (RADA)₄ were characterized over time. Sites of high (glycine-proline-glutamine-glycine+isoleucine-alanine-serine-glutamine (GPQG+IASQ), CP1) and low (glycine-proline-gl...Continue Reading

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Citations

Nov 21, 2018·Biomacromolecules·Kyle M KossLarry D Unsworth

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Methods Mentioned

BETA
transmission
scanning electron microscopy

Software Mentioned

Agitlent
MATLAB

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