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Tapping a bacterial enzymatic pathway for the preparation and manipulation of synthetic nanomaterials.

ABSTRACT: We present a spherical micelle generated in a three-step sequence in which a farnesyl-pantetheine conjugate is phosphorylated, adenylated, and phosphorylated once more to generate a farnesyl-CoA amphiphile that self-assembles into spherical micelles. A sphere-to-fibril morphological switch is achieved by enzymatically transferring the farnesyl group of the farnesyl-CoA micelle onto a peptide via phosphopantetheinyl transferase to generate a peptide amphiphile. Each step in the sequence is followed with characterization by HPLC, MS, TEM, and DLS. This system offers an entry into cofactor-mediated peptide decoration by extending the principles of bioresponsive polymeric materials to sequential enzyme cascades.

SUBMITTER: Ku TH

PROVIDER: S-EPMC6407424 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature

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Tapping a bacterial enzymatic pathway for the preparation and manipulation of synthetic nanomaterials.

Ku Ti-Hsuan TH Sahu Swagat S Kosa Nicolas M NM Pham Kevin M KM Burkart Michael D MD Gianneschi Nathan C NC

Journal of the American Chemical Society 20141203 50

We present a spherical micelle generated in a three-step sequence in which a farnesyl-pantetheine conjugate is phosphorylated, adenylated, and phosphorylated once more to generate a farnesyl-CoA amphiphile that self-assembles into spherical micelles. A sphere-to-fibril morphological switch is achieved by enzymatically transferring the farnesyl group of the farnesyl-CoA micelle onto a peptide via phosphopantetheinyl transferase to generate a peptide amphiphile. Each step in the sequence is follow ...[more]

PMID: 25468257

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