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Amphiphilic 4-helix bundles designed for biomolecular materials applications.

TitleAmphiphilic 4-helix bundles designed for biomolecular materials applications.
Publication TypeJournal Article
Year of Publication2004
AuthorsYe, S, Strzalka, JW, Discher, BM, Noy, D, Zheng, S, P Dutton, L, J Blasie, K
Date Published2004 Jul 06
KeywordsAmino Acid Motifs, Binding Sites, Heme, Oxidation-Reduction, Peptides, Pressure, Protein Structure, Secondary, Sensitivity and Specificity, Spectrophotometry, Ultraviolet, Surface Properties, Surface-Active Agents, X-Ray Diffraction

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.

Alternate JournalLangmuir
PubMed ID16459607
Grant ListGM41048 / GM / NIGMS NIH HHS / United States
GM48130 / GM / NIGMS NIH HHS / United States
GM55876 / GM / NIGMS NIH HHS / United States
GM63388 / GM / NIGMS NIH HHS / United States

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