169 Polymorphic assembly of computationally designed hydrophobic-rich collagen peptides |
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| Authors: | Kenneth N McGuinness Vikas Nanda |
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| Institution: | 1. Department of Biochemistry , UMDNJ/Rutgers University, Center for Advanced Biotechnology and Medicine , 679 Hoes Lane, Piscataway , NJ , 08854 , USA Phone: Phone: +1 928-925-7693 Fax: Phone: +1 928-925-7693 kennethm@eden.rutgers.edu;3. Department of Biochemistry , UMDNJ/Rutgers University, Center for Advanced Biotechnology and Medicine , 679 Hoes Lane, Piscataway , NJ , 08854 , USA Phone: Phone: +1 928-925-7693 Fax: Phone: +1 928-925-7693 |
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| Abstract: | 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 aggregation1 (DLA) (Parkinson et al. 1995). of discretized, rigid rods composed of hydrophilic and hydrophobic spheres. Simulations predicted that 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 and the peptide with five residues assembled into both fibrils and plates, while including four hydrophobic residues that formed only plates. This polymorphic behavior can be explained by packing models of rod vs. screw-like-particles. | |
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