Self-assembly of peptide porphyrin complexes: toward the development of smart biomaterials.
The anionic porphyrin, meso-tetrakis(4-sulfonatophenyl)porphine, is found to tightly bind to an engineered 14-residue peptide, resulting in induced alpha-helix formation when mixed in aqueous solutions. The small porphyrin-peptide dissociation constant (2 muM) observed is related to the energetics of peptide helix formation coupled with electrostatic interactions between the anionic porphyrin and cationic residues in the coiled peptide. Analytical ultracentrifugation measurements indicate the porphyrin-peptide complexes dimerize, probably into a coiled coil, and weakly associate to form even higher order structures.
Department of Biology, Haverford College, Pennsylvania 19041, USA.
Brian C
BC
Kovaric
Bashkim
B
Kokona
Alexander D
AD
Schwab
Margaret A
MA
Twomey
Julio C
JC
de Paula
Robert
R
Fairman
D000595:Amino Acid Sequence; D001672:Biocompatible Materials / Q000737:chemistry; D002942:Circular Dichroism; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011166:Porphyrins / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet; D055672:Static Electricity
D001672:Biocompatible Materials; D010455:Peptides; D011166:Porphyrins; C016136:tetraphenylporphine sulfonate