8T0I

Backbone Dialkylation in Peptide Hairpins: (R)-Ethylpropylglycine variant

8T0I の概要

• エントリーDOI: 10.2210/pdb8t0i/pdb
• NMR情報: BMRB: 31091
• 分子名称: Immunoglobulin G-binding protein G (1 entity in total)
• 機能のキーワード: hairpin, peptidomimetic, backbone modification, de novo protein
• 由来する生物種: Streptococcus sp. group G
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1883.07

構造登録者

Heath, S.L.,Horne, W.S.,Lengyel, G.A. (登録日: 2023-06-01, 公開日: 2023-08-16, 最終更新日: 2023-11-15)

主引用文献

Heath, S.L.,Horne, W.S.,Lengyel, G.A.
Effects of chirality and side chain length in C alpha , alpha-dialkylated residues on beta-hairpin peptide folded structure and stability.
Org.Biomol.Chem., 21:6320-6324, 2023

PubMed Abstract: Strategic incorporation of achiral C-dialkylated amino acids with bulky substituents into peptides can be used to promote extended strand conformations and inhibit protein-protein interactions associated with amyloid formation. In this work, we evaluate the thermodynamic impact of chiral C monomers on folding preferences in such systems through introduction of a series of C-methylated and C-ethylated residues into a β-hairpin host sequence. Depending on stereochemical configuration of the artificial monomer and potential for additional hydrophobic packing, a C-ethyl-C-propyl glycine residue can provide similar or enhanced folded stability relative to an achiral C-diethyl analogue.

PubMed: 37503895
DOI: 10.1039/d3ob00963g

実験手法

SOLUTION NMR