Structural highlights
Publication Abstract from PubMed
Peptide backbone N-amination has emerged as a useful strategy to stabilize antiparallel beta-sheet structure. Here, we used circular dichroism and NMR to evaluate the impact of amide-to-hydrazide substitution on the folded population of a parallel beta-hairpin model. Outer-edge N-amination was well tolerated and resulted in enhanced stability relative to N-methylation. High-resolution NMR structures confirmed that the alpha-hydrazino acid residues adopt canonical parallel beta-strand torsions that are compatible with the formation of intraresidue C6 hydrogen bonds involving the hydrazide NH(2) group.
Impact of Strand Edge N-Amination on the Stability of a Parallel beta-Hairpin Fold.,Starnes SK, Horne WS, Del Valle JR J Org Chem. 2025 Nov 20. doi: 10.1021/acs.joc.5c02479. PMID:41264875[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Starnes SK, Horne WS, Del Valle JR. Impact of Strand Edge N-Amination on the Stability of a Parallel β-Hairpin Fold. J Org Chem. 2025 Nov 20. PMID:41264875 doi:10.1021/acs.joc.5c02479
