Correction: Total synthesis of fellutamides, lipopeptide proteasome inhibitors. More sustainable peptide bond formation.

Correction for 'Total synthesis of fellutamides, lipopeptide proteasome inhibitors. More sustainable peptide bond formation' by Michael C. Pirrung, et al.

Total synthesis of fellutamides, lipopeptide proteasome inhibitors. More sustainable peptide bond formation.

Solution-phase syntheses of three bioactive natural products of mixed polypeptide-polyketide biogenesis, fellutamides A, B, and C, have been achieved. Three peptide bonds are generated without the use of coupling reagents in each synthesis of the fellutamides, which act against proteasomes.

Syrbactin Structural Analog TIR-199 Blocks Proteasome Activity and Induces Tumor Cell Death.

Multiple myeloma is an aggressive hematopoietic cancer of plasma cells. The recent emergence of three effective FDA-approved proteasome-inhibiting drugs, bortezomib (Velcade®), carfilzomib (Kyprolis®), and ixazomib (Ninlaro®), confirms that proteasome inhibitors are therapeutically useful against neoplastic disease, in particular refractory multiple myeloma and mantle cell lymphoma. This study describes the synthesis, computational affinity assessment, and preclinical evaluation of TIR-199, a natural product-derived syrbactin structural analog.

Total synthesis of bengazole A.

The divergent and enantioselective total synthesis of the powerful antifungal marine natural product bengazole A has been achieved.

RDC enhanced NMR spectroscopy in organic solvent media: the importance for the experimental determination of periodic hydrogen bonded secondary structures.

Precise NMR structural determination of distinct hydrogen-bonded secondary folds in unnatural peptides is demonstrated by using residual dipolar couplings (RDCs), measured in organic solvent media. The results show that the conventional constraints, (3)J(HH) and NOE-derived distances alone do not allow the accurate structural elucidation even for rigid foldamers and emphasize the need of RDC-based structure validation and refinement for unnatural peptides in particular and small organic molecules in general.

Oligomers of cis-beta-norbornene amino acid: formation of beta-strand mimetics.

The oligomers of constrained cis-exo-beta-norbornene amino acid were synthesised and characterised by extensive NMR, CD, IR and MD studies. The results showed the formation of both right and left handed consecutive 6-membered hydrogen-bonded strands for [2S,3R] and [2R,3S] enantiomers, respectively.