Using alpha-helical coiled-coils to design nanostructured metalloporphyrin arrays.
We have developed a computational design strategy based on the alpha-helical coiled-coil to generate modular peptide motifs capable of assembling into metalloporphyrin arrays of varying lengths. The current study highlights the extension of a two-metalloporphyrin array to a four-metalloporphyrin array through the incorporation of a coiled-coil repeat unit. Molecular dynamics simulations demonstrate that the initial design evolves rapidly to a stable structure with a small rmsd compared to the original model. Biophysical characterization reveals elongated proteins of the desired length, correct cofactor stoichiometry, and cofactor specificity. The successful extension of the two-porphyrin array demonstrates how this methodology serves as a foundation to create linear assemblies of organized electrically and optically responsive cofactors.
McAllister
Karen A
KA
Department of Biochemistry and Molecular Biophysics, Johnson Foundation, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Zou
Hongling
H
Cochran
Frank V
FV
Bender
Gretchen M
GM
Senes
Alessandro
A
Fry
H Christopher
HC
Nanda
Vikas
V
Keenan
Patricia A
PA
Lear
James D
JD
Saven
Jeffery G
JG
Therien
Michael J
MJ
Blasie
J Kent
JK
DeGrado
William F
WF
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D003198:Computer Simulation; D004578:Electron Spin Resonance Spectroscopy; D005290:Ferric Compounds / Q000138:chemical synthesis / Q000737:chemistry; D008665:Metalloporphyrins / Q000138:chemical synthesis / Q000737:chemistry*; D008958:Models, Molecular; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D008970:Molecular Weight; D049329:Nanostructures / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics
D005290:Ferric Compounds; D008665:Metalloporphyrins; D010455:Peptides