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. Author manuscript; available in PMC: 2014 Dec 9.
Published in final edited form as: Methods Mol Biol. 2013;1081:167–194. doi: 10.1007/978-1-62703-652-8_11

Fig 4.

Fig 4

Modular structures of (top) sandwiched associated triple-helical peptide and (bottom) sandwiched associated triple-helical peptide-amphiphile. The associated THP features repeats of Gly-Pro-Hyp [(GPO)n] on both the N- and C-termini to induce or stabilize triple-helical structure, and a diverse collagen-like sequence [(GXY)n] in the middle for structural and/or biological studies. The peptide-amphiphile additionally possesses a pseudo-lipid attached to the N-terminus to further enhance triple-helical stability via hydrophobic interactions