Based on the Improved K-Means Algorithm of Tianjin Port Traffic Flow Characteristic Analysis

Zhang, Yan; Yan, Xinping; Huang, Ming; Xie, Lei; Wang, Zheyue

doi:10.1061/41177(415)235

Cited by 2 publications

(1 citation statement)

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“…8,10,[14][15][16][17] In some cases, membrane-active AMPs employ cell-penetrating rather than permeabilizing properties to kill cells: after translocating across cell membranes, they damage intracellular targets. 16,[18][19] We recently identified significant differences in permeabilization strengths between piscidin 1 (p1, FFHHIFRGIVHVGKTIHRLVTG) and piscidin 3 (p3, FIHHIFRGIVHAGRSIGRFLTG), two homologous and α-helical AMPs from fish. 16,[37][38][39][40][41][42] The peptides are differentially-expressed, with p3, the less hemolytic isoform, more preponderant in vascularized tissues.…”

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confidence: 99%

Structure and Function in Antimicrobial Piscidins: Histidine Position, Directionality of Membrane Insertion, and pH-Dependent Permeabilization

et al. 2019

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Piscidins are histidine-enriched antimicrobial peptides that interact with lipid bilayers as amphipathic α-helices. Their activity at acidic and basic pH in vivo makes them promising templates for biomedical applications. This study focuses on p1 and p3, both 22-residue-long piscidins with 68% sequence identity. They share three histidines (H3, H4 and H11) but p1, which is significantly more permeabilizing, has a fourth histidine (H17). This study investigates how variations in amphipathic character associated with histidines affect the permeabilization properties of p1 and p3. First, we show that the permeabilization ability of p3, but not p1, is strongly inhibited at pH 6.0 when the conserved histidines are partially charged and H17 is

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