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Self Assembly of Coiled-Coil Peptide−Porphyrin Complexes
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    Self Assembly of Coiled-Coil Peptide−Porphyrin Complexes
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    Department of Biology, Haverford College, 370 Lancaster Avenue, Haverford, Pennsylvania 19041
    * To whom correspondence should be addressed. Tel.: (610) 896-4205. Fax: (610) 896-4963. E-mail: [email protected]
    §Current Address: Department of Chemistry, Lewis and Clark College, 0615 SW Palatine Hill Rd., Portland, OR 97219.
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    Biomacromolecules

    Cite this: Biomacromolecules 2009, 10, 6, 1454–1459
    Click to copy citationCitation copied!
    https://doi.org/10.1021/bm9000553
    Published April 17, 2009
    Copyright © 2009 American Chemical Society

    Abstract

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    We are interested in the controlled assembly of photoelectronic materials using peptides as scaffolds and porphyrins as the conducting material. We describe the integration of a peptide-based polymer strategy with the ability of designed basic peptides to bind anionic porphyrins in order to create regulated photoelectronically active biomaterials. We have described our peptide system in earlier work, which demonstrates the ability of a peptide to form filamentous materials made up of self-assembling coiled-coil structures. We have modified this peptide system to include lysine residues appropriately positioned to specifically bind meso-tetrakis(4-sulfonatophenyl)porphine (TPPS4), a porphyrin that contains four negatively charged sulfonate groups at neutral pH. We measure the binding of TPPS4 to our peptide using UV−visible and fluorescence spectroscopies to follow the porphyrin signature. We determine the concomitant acquisition of helical secondary structure in the peptide upon TPPS4 binding using circular dichroism spectropolarimetry. This binding fosters polymerization of the peptide, as shown by absorbance extinction effects in the peptide CD spectra. The morphologies of the peptide/porphyrin complexes, as imaged by atomic force microscopy, are consistent with the coiled-coil polymers that we had characterized earlier, except that the heights are slightly higher, consistent with porphyrin binding. Evidence for exciton coupling in the copolymers is shown by red-shifting in the UV−visible data, however, the coupling is weak based on a lack of fluorescence quenching in fluorescence experiments.

    Copyright © 2009 American Chemical Society

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    Atomic force microscopy image of Cp3K in 0.1 M NaCl and circular dichroism spectrum and atomic force microscopy image of Cp3K peptide forming cross-β-sheet fibrils. This material is available free of charge via the Internet at http://pubs.acs.org.

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    Cited By

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    This article is cited by 47 publications.

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    Biomacromolecules

    Cite this: Biomacromolecules 2009, 10, 6, 1454–1459
    Click to copy citationCitation copied!
    https://doi.org/10.1021/bm9000553
    Published April 17, 2009
    Copyright © 2009 American Chemical Society

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