6RQS

RW16 peptide

6RQS の概要

• エントリーDOI: 10.2210/pdb6rqs/pdb
• NMR情報: BMRB: 34400
• 分子名称: ARG-ARG-TRP-ARG-ARG-TRP-TRP-ARG-ARG-TRP-TRP-ARG-ARG-TRP-ARG-ARG (1 entity in total)
• 機能のキーワード: arginine, tryptophan, membrane, cell-penetrating, membrane 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: 3032.64

構造登録者

Jobin, M.-L.,Grelard, A.,Alves, I.,Mackereth, C.D. (登録日: 2019-05-16, 公開日: 2019-10-23, 最終更新日: 2024-06-19)

主引用文献

Jobin, M.L.,Vamparys, L.,Deniau, R.,Grelard, A.,Mackereth, C.D.,Fuchs, P.F.J.,Alves, I.D.
Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide.
Int J Mol Sci, 20:-, 2019

PubMed Abstract: Cell-penetrating peptides (CPPs) are short peptides that can translocate and transport cargoes into the intracellular milieu by crossing biological membranes. The mode of interaction and internalization of cell-penetrating peptides has long been controversial. While their interaction with anionic membranes is quite well understood, the insertion and behavior of CPPs in zwitterionic membranes, a major lipid component of eukaryotic cell membranes, is poorly studied. Herein, we investigated the membrane insertion of RW16 into zwitterionic membranes, a versatile CPP that also presents antibacterial and antitumor activities. Using complementary approaches, including NMR spectroscopy, fluorescence spectroscopy, circular dichroism, and molecular dynamic simulations, we determined the high-resolution structure of RW16 and measured its membrane insertion and orientation properties into zwitterionic membranes. Altogether, these results contribute to explaining the versatile properties of this peptide toward zwitterionic lipids.

PubMed: 31505894
DOI: 10.3390/ijms20184441

実験手法

SOLUTION NMR