The tunable self-assembly of short oligomeric peptide sequences into ordered supramolecular architectures has become an increasingly versatile scaffold for cell culturing, biosensing, display technology, and the incorporation of therapeutic agents.1,2,3 Flanking hydrophobic peptide residues with aromatic substituents provides additional intermolecular ?-stacking leading to aggregation and hydrogelation.4,5 We constructed mono- and di-peptide sequences containing hydrophobic amino acid residues (Valine, Phenylalanine, etc.) capped with two variant naphthalene compounds to provide bi-functional fluorescent bioconjugates with new optoelectronic properties and directionality during hierarchical self-assembly. The self-assembly patterns of the various mono- and bi-functional naphthalene-peptides were compared under various stimuli: solvents composition, sonication, solution pH, ion addition, and temperature. The synthesized bioconjugates were characterized in solution and solid state by various analytical techniques: fluorescence, IR, CD, and UV-Vis spectroscopies, NMR, X-ray diffraction and electron microscopy to gain insight into their structural features, photophysical properties and self-assembling motifs.Y. Zhang, H. W. Gu, Z. M. Yang and B. Xu, J. Am. Chem. Soc., 2003, 125, 13680.F. M. Menger and K. L. Caran, J. Am. Chem. Soc., 2000, 122, 11679.A. Heeres, C. Van der Pol, M. Stuart, A. Friggeri, B. L. Feringa and J. Van Esch, J. Am. Chem. Soc., 2003, 125, 14252Z. Yang, Bing Xu, Chem. Commun., 2006, 738-740Y. Kuang, Y. Gao, B. Xu, Chem. Commun., 2011, 12625-12627

Exploration of naphthalene capped hydrophobic di-peptide self-assembling motifs

248th National Meeting (2014)

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