5zvf

Structure of [T9,K7]indolicidin, a non glycosylated analogue of indolicidin

spinqualitylabelsall models 5zvf Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zvf is a 1 chain structure with sequence from Bos taurus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CTHL4_BOVIN Potent microbicidal activity; active against S.aureus and E.coli. Publication Abstract from PubMed 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, [betaGlc-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. Design of therapeutically improved analogue of the antimicrobial peptide, indolicidin, using a glycosylation strategy.,Dwivedi R, Aggarwal P, Bhavesh NS, Kaur KJ Amino Acids. 2019 Nov;51(10-12):1443-1460. doi: 10.1007/s00726-019-02779-2. Epub , 2019 Sep 4. PMID:31485742 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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