7OSD

NMR Solution Structure of Peptide 12: First-in-class cyclic Temporin L analogue with antibacterial and antibiofilm activities

7OSD の概要

• エントリーDOI: 10.2210/pdb7osd/pdb
• NMR情報: BMRB: 34634
• 分子名称: PHE-VAL-PRO-TRP-PHE-LYS-LYS-PHE-DLE-GLU-ARG-ILE-LEU-NH2 (1 entity in total)
• 機能のキーワード: temporins, antimicrobial, antimicrobial protein
• 由来する生物種: Rana temporaria
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1724.14

構造登録者

Brancaccio, D.,Carotenuto, A. (登録日: 2021-06-08, 公開日: 2021-08-11, 最終更新日: 2024-11-06)

主引用文献

Bellavita, R.,Casciaro, B.,Di Maro, S.,Brancaccio, D.,Carotenuto, A.,Falanga, A.,Cappiello, F.,Buommino, E.,Galdiero, S.,Novellino, E.,Grossmann, T.N.,Mangoni, M.L.,Merlino, F.,Grieco, P.
First-in-Class Cyclic Temporin L Analogue: Design, Synthesis, and Antimicrobial Assessment.
J.Med.Chem., 64:11675-11694, 2021

PubMed Abstract: The pharmacodynamic and pharmacokinetic properties of bioactive peptides can be modulated by introducing conformational constraints such as intramolecular macrocyclizations, which can involve either the backbone and/or side chains. Herein, we aimed at increasing the α-helicity content of temporin L, an isoform of an intriguing class of linear antimicrobial peptides (AMPs), endowed with a wide antimicrobial spectrum, by the employment of diverse side-chain tethering strategies, including lactam, 1,4-substituted [1,2,3]-triazole, hydrocarbon, and disulfide linkers. Our approach resulted in a library of cyclic temporin L analogues that were biologically assessed for their antimicrobial, cytotoxic, and antibiofilm activities, leading to the development of the first-in-class cyclic peptide related to this AMP family. Our results allowed us to expand the knowledge regarding the relationship between the α-helical character of temporin derivatives and their biological activity, paving the way for the development of improved antibiotic cyclic AMP analogues.

PubMed: 34296619
DOI: 10.1021/acs.jmedchem.1c01033

実験手法

SOLUTION NMR