Fig. 1: Self-assembly and structural characterization of Hyp-Phe-Phe. | Nature Communications

Fig. 1: Self-assembly and structural characterization of Hyp-Phe-Phe.

From: Molecular engineering of piezoelectricity in collagen-mimicking peptide assemblies

Fig. 1

a Chemical structure of Pro-Phe-Phe and Hyp-Phe-Phe. b FTIR analysis of Hyp-Phe-Phe assemblies showing the characteristic peak of helical conformation. c CD spectrum of the tripeptide reveals the presence of helical assemblies in solution. d AFM image of the tripeptide demonstrating fibrillar morphology. e TEM image of the tripeptide fibres. f Single-crystal structure of Hyp-Phe-Phe showing the formation of an elongated structure by stacking of helices through intermolecular hydrogen bonding and aromatic zipper-like packing. CCDC ref. no. 182336726. g, h Mechanical strength of the Hyp-Phe-Phe fibres. g Nanoscale mapping of Young’s modulus (Z-scale = 140 GPa). h Line section through one fibril as highlighted by the green line in g, showing the periodic variation in stiffness along the fibril. Additional AFM and TEM data are given in Supplementary Figs. 13.

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