192057-94-6Relevant articles and documents
The unique crystallographic signature of a β-turn mimic nucleated by N-methylated phenylalanine and Aib as corner residue: Conformational and self-assembly studies
Konar, Anita Dutt
, p. 10569 - 10578 (2013)
The secondary α-amino acid, proline, having high β-turn forming propensity is known to stabilize discrete conformations in peptides. A similar influence is ascribed to N-methylated amino acids with the advantage of the introduction of a side chain functio
Divergent Access to Histone Deacetylase Inhibitory Cyclopeptides via a Late-Stage Cyclopropane Ring Cleavage Strategy. Short Synthesis of Chlamydocin
Elek, Gábor Zoltán,Koppel, Kaur,Zubrytski, Dzmitry M.,Konrad, Nele,J?rving, Ivar,Lopp, Margus,Kananovich, Dzmitry G.
supporting information, p. 8473 - 8478 (2019/10/16)
A unified step-economical strategy for accessing histone deacetylase inhibitory peptides is proposed, based on the late-stage installation of multiple zinc-binding functionalities via the cleavage of the strained cyclopropane ring in the common pluripoten
Diversity of Secondary Structure in Catalytic Peptides with β-Turn-Biased Sequences
Metrano, Anthony J.,Abascal, Nadia C.,Mercado, Brandon Q.,Paulson, Eric K.,Hurtley, Anna E.,Miller, Scott J.
supporting information, p. 492 - 516 (2017/02/23)
X-ray crystallography has been applied to the structural analysis of a series of tetrapeptides that were previously assessed for catalytic activity in an atroposelective bromination reaction. Common to the series is a central Pro-Xaa sequence, where Pro is either l- or d-proline, which was chosen to favor nucleation of canonical β-turn secondary structures. Crystallographic analysis of 35 different peptide sequences revealed a range of conformational states. The observed differences appear not only in cases where the Pro-Xaa loop-region is altered, but also when seemingly subtle alterations to the flanking residues are introduced. In many instances, distinct conformers of the same sequence were observed, either as symmetry-independent molecules within the same unit cell or as polymorphs. Computational studies using DFT provided additional insight into the analysis of solid-state structural features. Select X-ray crystal structures were compared to the corresponding solution structures derived from measured proton chemical shifts, 3J-values, and 1H-1H-NOESY contacts. hese findings imply that the conformational space available to simple peptide-based catalysts is more diverse than precedent might suggest. The direct observation of multiple ground state conformations for peptides of this family, as well as the dynamic processes associated with conformational equilibria, underscore not only the challenge of designing peptide-based catalysts, but also the difficulty in predicting their accessible transition states. These findings implicate the advantages of low-barrier interconversions between conformations of peptide-based catalysts for multistep, enantioselective reactions.
