Albany 2013: Book of Abstracts
June 11-15 2013
©Adenine Press (2012)
Polymorphic assembly of computationally designed hydrophobic-rich collagen peptides
We seek to understand how the position and length of hydrophobic content within a collagen peptide sequence dictates morphology of self-assembly. We modeled collagen assembly using diffusion limited aggregation (DLA) (Parkinson et al. 1995) of discretized, rigid rods composed of hydrophilic and hydrophobic spheres. Simulations predicted the inclusion of short hydrophobic domains should direct the assembly of lamellar structures. We designed a set of collagen peptide sequences with six, five and four contiguous nonpolar residues. Electron microscopy of aggregates revealed the peptide with six nonpolar residues self-assembled into uniform fibrils, the peptide with five residues assembled into both fibrils and plates, while including four hydrophobic residues formed only plates. This polymorphic behavior can be explained by packing models of rod versus screw-like-particles.
This research has been supported by NSF DMR-0907273 and NIH DP2-OD-006478-1.
Parkinson, J., Kadler, K. E., & Brass, A. (1995). Simple physical model of collagen fibrillogenesis based on diffusion limited aggregation. Journal of molecular biology, 247(4), 823-831.
Kenneth N. McGuinness
Department of Biochemistry