Journal
JOURNAL OF THE BRAZILIAN CHEMICAL SOCIETY
Volume 21, Issue 7, Pages 1390-1394Publisher
SOC BRASILEIRA QUIMICA
DOI: 10.1590/S0103-50532010000700027
Keywords
cobalt protoporphyrin IX; peptides; fibers; self-assembly
Categories
Funding
- NSF [CHE-0455441]
- ACS-PRF [34901]
- CAPES [4174/08-9]
Ask authors/readers for more resources
The polypeptide H21(30-mer) folds into a two-stranded coiled-coil in which two solvent-exposed histidine residues reside on opposite sides of its surface. This peptide was allowed to react with cobalt(III) protoporphyrin IX, Co(ppIX), to produce [Co(ppIX){(H21(30-mer)}(2)], as determined by UV-Vis spectroscopy. This bis-axial ligation thus positions a potential coiled-coil oligomerization domain onto each face of the cobalt porphyrin ring. Circular dichroism spectroscopy and high performance size exclusion chromatography provide evidence for the solution-phase self-assembly of these porphyrin-peptide units. Evaporation of the porphyrin-peptide solution on a solid support results in the formation of long rod-like materials having millimeter-scale lengths and micron-scale diameters. The presence of Co(ppIX) in these materials was confirmed by Raman microscopy. However, they were formed only from phosphate buffer, and not from organic buffers or pure water, indicating that their formation might involve a more complicated process than originally anticipated.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available