Send to

Choose Destination
See comment in PubMed Commons below
Biomacromolecules. 2011 Dec 12;12(12):4196-203. doi: 10.1021/bm201354m. Epub 2011 Nov 7.

Characterization of mesoscale coiled-coil peptide-porphyrin complexes.

Author information

  • 1Department of Biology, Haverford College, Haverford, Pennsylvania 19041, United States.


Photoelectronically conductive self-assembling peptide-porphyrin assemblies have great potential in their use as biomaterials, owing largely to their environmentally responsive properties. We have successfully designed a coiled-coil peptide that can self-assemble to form mesoscale filaments and serve as a scaffold for porphyrin interaction. In our earlier work, peptide-porphyrin-based biomaterials were formed at neutral pH, but the structures were irregular at the nano- to microscale size range, as judged by atomic force microscopy. We identified a pH in which mesoscale fibrils were formed, taking advantage of the types of porphyrin interactions that are present in well-characterized J-aggregates. We used UV-visible spectroscopy, circular dichroism spectropolarimetry, fluorescence spectroscopy, and atomic force microscopy to characterize these self-assembling biomaterials. We propose a new assembly paradigm that arises from a set of unique porphyrin-porphyrin and porphyrin-peptide interactions whose structure may be readily modulated by changes in pH or peptide concentration.

[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for American Chemical Society
    Loading ...
    Support Center