Nanometer to millimeter scale peptide-porphyrin materials.

Abstract:

:AQ-Pal14 is a 30-residue polypeptide that was designed to form an α-helical coiled coil that contains a metal-binding 4-pyridylalanine residue on its solvent-exposed surface. However, characterization of this peptide shows that it exists as a three-stranded coiled coil, not a two-stranded one as predicted from its design. Reaction with cobalt(III) protoporphyrin IX (Co-PPIX) produces a six-coordinate Co-PPIX(AQ-Pal14)(2) species that creates two coiled-coil oligomerization domains coordinated to opposite faces of the porphyrin ring. It is found that this species undergoes a buffer-dependent self-assembly process: nanometer-scale globular materials were formed when these components were reacted in unbuffered H(2)O, while millimeter-scale, rod-like materials were prepared when the reaction was performed in phosphate buffer (20 mM, pH 7). It is suggested that assembly of the globular material is dictated by the conformational properties of the coiled-coil forming AQ-Pal14 peptide, whereas that of the rod-like material involves interactions between Co-PPIX and phosphate ion.

journal_name

Biomacromolecules

journal_title

Biomacromolecules

authors

Zaytsev DV,Xie F,Mukherjee M,Bludin A,Demeler B,Breece RM,Tierney DL,Ogawa MY

doi

10.1021/bm100540t

subject

Has Abstract

pub_date

2010-10-11 00:00:00

pages

2602-9

issue

10

eissn

1525-7797

issn

1526-4602

journal_volume

11

pub_type

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