Design, synthesis and properties of synthetic chlorophyll proteins.
A chemoselective method is described for coupling chlorophyll derivatives with an aldehyde group to synthetic peptides or proteins modified with an aminoxyacetyl group at the epsilon-amino group of a lysine residue. Three template-assembled antiparallel four-helix bundles were synthesized for the ligation of one or two chlorophylls. This was achieved by coupling unprotected peptides to cysteine residues of a cyclic decapeptide by thioether formation. The amphiphilic helices were designed to form a hydrophobic pocket for the chlorophyll derivatives. Chlorophyll derivatives Zn-methyl-pheophorbide b and Zn-methyl-pyropheophorbide d were used. The aldehyde group of these chlorophyll derivatives was ligated to the modified lysine group to form an oxime bond. The peptide-chlorophyll conjugates were characterized by electrospray mass spectrometry, analytical HPLC, and UV/visible spectroscopy. Two four-helix bundle chlorophyll conjugates were further characterized by size-exclusion chromatography, circular dichroism, and resonance Raman spectroscopy.
Rau
H K
HK
Institut für Biologie II/Biochemie, Albert-Ludwigs-Universität Freiburg, Germany.
Snigula
H
H
Struck
A
A
Robert
B
B
Scheer
H
H
Haehnel
W
W
D000595:Amino Acid Sequence; D002734:Chlorophyll / Q000031:analogs & derivatives*; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D015195:Drug Design; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis; D010940:Plant Proteins / Q000138:chemical synthesis* / Q000737:chemistry; D013053:Spectrophotometry; D013059:Spectrum Analysis, Raman
D010455:Peptides; D010940:Plant Proteins; D002734:Chlorophyll