6E5H

Heterogeneous-Backbone Mimics of a Designed Disulfide-Rich Protein: Aib turn

6E5H の概要

• エントリーDOI: 10.2210/pdb6e5h/pdb
• NMR情報: BMRB: 30496
• 分子名称: Designed peptide NC_HEE_D1: Aib turn mutant (1 entity in total)
• 機能のキーワード: heterogeneous backbone foldamer, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3260.81

構造登録者

Cabalteja, C.C.,Mihalko, D.S.,Horne, W.S. (登録日: 2018-07-20, 公開日: 2018-11-21, 最終更新日: 2023-06-14)

主引用文献

Cabalteja, C.C.,Mihalko, D.S.,Horne, W.S.
Heterogeneous-Backbone Foldamer Mimics of a Computationally Designed, Disulfide-Rich Miniprotein.
Chembiochem, 20:103-110, 2019

PubMed Abstract: Disulfide-rich peptides have found widespread use in the development of bioactive agents; however, low proteolytic stability and the difficulty of exerting synthetic control over chain topology present barriers to their application in some systems. Herein, we report a method that enables the creation of artificial backbone ("foldamer") mimics of compact, disulfide-rich tertiary folds. Systematic replacement of a subset of natural α-residues with various artificial building blocks in the context of a computationally designed prototype sequence leads to "heterogeneous-backbone" variants that undergo clean oxidative folding, adopt tertiary structures indistinguishable from that of the prototype, and enjoy proteolytic protection beyond that inherent to the topologically constrained scaffold. Collectively, these results demonstrate systematic backbone substitution to be a viable method to engineer the properties of disulfide-rich sequences and expands the repertoire of protein mimicry by foldamers to an exciting new structural class.

PubMed: 30326175
DOI: 10.1002/cbic.201800558

実験手法

SOLUTION NMR