牛血红蛋白源抗菌肽P3及其类似肽的生物信息学分析

doi:10.16431/j.cnki.1671-7236.2017.01.008

Abstract

Abstract:

To provide basic information for researching the biological function of antimicrobial peptide P3 from bovine hemoglobin and its analogs (JH-0, JH-1, JH-2 and JH-3), tools on line were utilized to analyze some bioinformatic features of these five peptides. The results showed that the isoelectric point of these five peptides were all more than 8.00. All of these five peptides had positive charge, no transmembrane domain, no signal peptide sequence, no glycosylation sites,were hydrophobins and located at extracellular. The secondary structure of peptide P3 and JH-2 had α-helix and β-sheet, JH-3 was all α-helix, while JH-0 and JH-1 were coil. Peptide P3, JH-2 and JH-3 had a glycosylation site at the thirteenth site of amino acid (Thr, T), respectively. Based on these results, we conjectured that antimicrobial peptide P3 and its analogs could kill bacteria through the interaction with cell wall or cell membrane.

Key words: bovine hemoglobin; antimicrobial peptide; analogous peptide; bioinformatics

CLC Number:

S859.79⁺7

LI Jie, HANG Bo-lin, QIN Ai-jian, QIAN Kun, HU Jian-he. Bioinformatics Analysis of Antimicrobial Peptide P3 from Bovine Hemoglobin and Its Analogs[J]. , 2017, 44(1): 59-64.

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Bioinformatics Analysis of Antimicrobial Peptide P3 from Bovine Hemoglobin and Its Analogs

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