Pentelute Lab MIT | Pentelute Lab MIT - Publications Page

The Pentelute Lab leverages expertise in peptide chemistry, molecular biology, and technology development to create peptide and protein-based therapeutics and tools for chemical biology.

Pentelute Lab, MIT, Cambridge, Chemistry, Molecular biology, technology development, peptide, protein-based therapeutics, chemical Biology, Bradley Pentelute

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PUBLICATIONS

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Publications

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Enzymatic “Click” Ligation: Selective Cysteine Modification in Polypeptides Enabled by Promiscuous Glutathione S-Transferase

2013, Publications

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Monitoring the Kinetics of the pH-Driven Transition of the Anthrax Toxin Prepore to the Pore by Biolayer Interferometry and Surface Plasmon Resonance.

2013, Publications

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PUBLICATIONS

A fully automated flow-based approach for accelerated peptide synthesis

Palladium-Mediated Arylation of Lysine in Unprotected Peptides

Salt Effect Accelerates Site-Selective Cysteine Bioconjugation

d-Amino Acid Scan of Two Small Proteins

Nitrogen Arylation for Macrocyclization of Unprotected Peptides

Delivery of Non-Native Cargo into Mammalian Cells Using Anthrax Lethal Toxin

Systematic Investigation of EDC/sNHS-Mediated Bioconjugation Reactions for Carboxylated Peptide Substrates

C-Terminal Modification of Fully Unprotected Peptide Hydrazides via in Situ Generation of Isocyanates

Macrocyclization of Unprotected Peptide Isocyanates

A perfluoroaromatic abiotic analog of H2 relaxin enabled by rapid flow-based peptide synthesis

π-Clamp-mediated cysteine conjugation

A d-Amino Acid at the N-Terminus of a Protein Abrogates Its Degradation by the N-End Rule Pathway

Organometallic palladium reagents for cysteine bioconjugation

An Umpolung Approach for the Chemoselective Arylation of Selenocysteine in Unprotected Peptides.

Translocation of Non-Canonical Polypeptides into Cells Using Protective Antigen

A functional role of Rv1738 in Mycobacterium tuberculosis persistence suggested by racemic protein crystallography

Atomic structure of anthrax protective antigen pore elucidates toxin translocation.

Total Synthesis and Biochemical Characterization of Mirror Image Barnase

Following Natures Lead: On the Construction of Membrane-Inserted Toxins in Lipid Bilayer Nanodiscs

Delivery of mirror image polypeptides into cells

Delivery of Antibody Mimics into Mammalian Cells via Anthrax Toxin Protective Antigen

Enzyme-Catalyzed Macrocyclization of Long Unprotected Peptides

Flow-Based Enzymatic Ligation via Sortase A

Rapid Total Synthesis of DARPin pE59 and Barnase

Rapid Flow-Based Peptide Synthesis

Convergent Diversity-Oriented Side-Chain Macrocyclization Scan for Unprotected Polypeptides

Enzymatic “Click” Ligation: Selective Cysteine Modification in Polypeptides Enabled by Promiscuous Glutathione S-Transferase

Monitoring the Kinetics of the pH-Driven Transition of the Anthrax Toxin Prepore to the Pore by Biolayer Interferometry and Surface Plasmon Resonance.

A Perfluoroaryl-Cysteine Chemistry Approach to Unprotected Peptide Stapling

Three Dimensional Structure of the Anthrax Toxin Translocon–lethal Factor Complex by Cryo-electron Microscopy

Evidence for a Common Mechanism of SIRT1 Regulation by Allosteric Activators

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

Protein Thioester Synthesis Enabled By: Sortase