Amphiphilic 4-helix bundles designed for biomolecular materials applications.
Artificial peptides previously designed to possess alpha-helical bundle motifs have been either hydrophilic (i.e., soluble in polar media) or lipophilic (i.e., soluble in nonpolar media) in overall character. Realizations of these bioinspired bundles have succeeded in reproducing a variety of biomimetic functionality within the appropriate media. However, to translate their functionality into any biomolecular device applications at the macroscopic level, the bundles must be oriented in an ensemble, for example, at an interface. This goal has been realized in a new family of alpha-helical bundle peptides which are amphiphilic; namely, they assemble into 4-helix bundles with well-defined hydrophilic and hydrophobic domains. These peptides are capable of binding metalloporphyrin prosthetic groups at selected locations within these domains. We describe here the realization of one of the first members of this family, AP0, successfully designed for vectorial incorporation into soft interfaces between polar and nonpolar media.
Ye
Shixin
S
Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Strzalka
Joseph W
JW
Discher
Bohdana M
BM
Noy
Dror
D
Zheng
Songyan
S
Dutton
P Leslie
PL
Blasie
J Kent
JK
D020816:Amino Acid Motifs; D001665:Binding Sites; D006418:Heme / Q000737:chemistry; D010084:Oxidation-Reduction; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011312:Pressure; D017433:Protein Structure, Secondary; D012680:Sensitivity and Specificity; D013056:Spectrophotometry, Ultraviolet / Q000379:methods; D013499:Surface Properties; D013501:Surface-Active Agents / Q000138:chemical synthesis / Q000737:chemistry*; D014961:X-Ray Diffraction / Q000379:methods
D010455:Peptides; D013501:Surface-Active Agents; D006418:Heme