Assembly of Anthrax Toxin Pore: Lethal-factor Complexes into Lipid Nanodiscs.
The Pentelute Lab aims to invent new chemistry for the efficient and selective modification of proteins, to ‘hijack’ these biological machines for efficient drug delivery into cells and to create new machines to rapidly and efficiently manufacture peptides and proteins.
Pentelute Lab, Chemistry, MIT, Chemistry Department, Boston, Cambridge, Biology, Peptides, Peptide, Proteins, Science, Rapid, Brad Pentelute, Brad,
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Assembly of Anthrax Toxin Pore: Lethal-factor Complexes into Lipid Nanodiscs.

Assembly of Anthrax Toxin Pore: Lethal-factor Complexes into Lipid Nanodiscs.

Akkaladevi, Hinton-Chollet, Katayama, Mitchell, Szerszen, Mukherjee, Gogol, Pentelute, Collier, Fisher, Protein Sci., 2013, 22:492-501

Abstract

We report the discovery of a facile transformation between perfluoroaromatic molecules and a cysteine thiolate, which is arylated at room temperature. This new approach enabled us to selectively modify cysteine residues in unprotected peptides, providing access to variants containing rigid perfluoroaromatic staples. This stapling modification performed on a peptide sequence designed to bind the C-terminal domain of an HIV-1 capsid assembly polyprotein (C- CA), showed enhancement in binding, cell permeability, and proteolytic stability properties, as compared to the unstapled analog. Importantly, chemical stability of the formed staples allowed us to use this motif in the native chemical ligation mediated synthesis of a small protein affibody that is capable of binding the Human Epidermal Growth Factor 2 (HER-2) receptor...

Published

Published online February, 7 2013

Category
2013, Publications