Abstract
Tachyplesin I (TP I) is an antimicrobial peptide isolated from the hemocytes of the horseshoe crab. With the developments of DNA microarray technology, the genetic analysis of the toxic effect of TP I on embryo was originally considered in our recent study. Based on our microarray data of the embryonic samples of zebrafish treated with the different doses of TP I, we performed a series of statistical data analyses to explore the toxic effect of TP I at the genomic level. In this paper, we first employed the hexaMplot to illustrate the continuous variation of the gene expressions of the embryonic cells treated with the different doses of TP I. The probabilistic model-based Hough transform was used to classify these differentially coexpressed genes of TP I on the zebrafish embryos. As a result, three line rays supported with the corresponding 174 genes were detected in our analysis. Some biological processes of the featured genes, such as antigen processing, nuclear chromatin, and structural constituent of eye lens, were significantly filtered with the smaller P values.
Highlights
Tachyplesin I (TP I) is originally isolated from the acid extracts of hemocytes of the horseshoe crab Tachypleus tridentatus in 1988 [1]
Among these 17 alpha amino acid residues, 4 cysteine residues constitute two disulfide bonds that contribute to the hemolytic ability of TP I in blood cells [2]
TP I was synthesized by Shenzhen Han Yu Pharmaceutical Co., Ltd. according to the sequence reported by Nakamura et al (1988) [1]
Summary
Tachyplesin I (TP I) is originally isolated from the acid extracts of hemocytes of the horseshoe crab Tachypleus tridentatus in 1988 [1]. TP I consists of 17 amino acid residues, two disulfide bonds, and one unique α-arginine at the C terminal end and is characterized by a disulfide-stabilized β-sheet conformation. Among these 17 alpha amino acid residues, 4 cysteine residues constitute two disulfide bonds that contribute to the hemolytic ability of TP I in blood cells [2]. The peptide interacts with DNA and inhibits the synthesis of macromolecules. Because of its potency and relatively small size, this peptide is a promising candidate of a novel alternative antibiotic in the pharmaceutical industry and animal and food industries. In comparison with the biochemical structure and mechanism of TP I, the literature on the toxicity of TP I is very limited, except its hemolytic ability
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