5ZVN

Structure of [beta Glc-T9,K7]indolicidin, a glycosylated analogue of indolicidin

5ZVN の概要

• エントリーDOI: 10.2210/pdb5zvn/pdb
• NMR情報: BMRB: 36190
• 分子名称: glycosylated analogue of Indolicidin, beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: antimicrobial indolicidin derivative, antimicrobial protein
• 由来する生物種: Bos taurus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2035.41

構造登録者

Dwivedi, R.,Aggarwal, P.,Kaur, K.J.,Bhavesh, N.S. (登録日: 2018-05-11, 公開日: 2019-06-19, 最終更新日: 2024-11-20)

主引用文献

Dwivedi, R.,Aggarwal, P.,Bhavesh, N.S.,Kaur, K.J.
Design of therapeutically improved analogue of the antimicrobial peptide, indolicidin, using a glycosylation strategy.
Amino Acids, 51:1443-1460, 2019

PubMed Abstract: Indolicidin is a member of cathelicidin family which displays broad spectrum antimicrobial activity. Severe toxicity and aggregation propensity associated with indolicidin pose a huge limitation to its probable therapeutic application. We are reporting the use of glycosylation strategy to design an analogue of indolicidin and subsequently explore structural and functional effects of sugar on it. Our study led to the design of a potent antibacterial glycosylated peptide, [βGlc-T9,K7]indolicidin, which showed decreased toxicity against erythrocytes and macrophage cells and thus a higher therapeutic selectivity. The incorporation of sugar also increased the solubility of the peptide. The mode of bacterial killing, functional stability, LPS binding, and cytokine inhibitory potential of the peptide, however, seemed unaffected upon glycosylation. Absence of significant changes in structure upon glycosylation accounts for the possibly retained functions and mode of action of the peptide. Our report thus presents the designing of an indolicidin analogue with improved therapeutic potential by substituting aromatic amino acid with glycosylated amino acid as a promising strategy for the first time.

PubMed: 31485742
DOI: 10.1007/s00726-019-02779-2

実験手法

SOLUTION NMR