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Open AccessArticle

Antibacterial Activity of AI-Hemocidin 2, a Novel N-Terminal Peptide of Hemoglobin Purified from Arca inflata

1
Biotechnological Institute of Chinese Materia Medica, Jinan University, Guangzhou 510632, China
2
National Engineering Research Center of Microsphere Technology for Controlled-Release Drug Delivery, Zhuhai 519090, China
3
Department of Pharmacology, Jinan University, Guangzhou 510632, China
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Mar. Drugs 2017, 15(7), 205; https://doi.org/10.3390/md15070205
Received: 23 April 2017 / Revised: 25 June 2017 / Accepted: 27 June 2017 / Published: 29 June 2017
(This article belongs to the Collection Bioactive Compounds from Marine Invertebrates)
The continued emergence of antibiotic resistant bacteria in recent years is of great concern. The search for new classes of antibacterial agents has expanded to non-traditional sources such as shellfish. An antibacterial subunit of hemoglobin (Hb-I) was purified from the mantle of Arca inflata by phosphate extraction and ion exchange chromatography. A novel antibacterial peptide, AI-hemocidin 2, derived from Hb-I, was discovered using bioinformatics analysis. It displayed antibacterial activity across a broad spectrum of microorganisms, including several Gram-positive and Gram-negative bacteria, with minimal inhibitory concentration (MIC) values ranging from 37.5 to 300 μg/mL, and it exhibited minimal hemolytic or cytotoxic activities. The antibacterial activity of AI-hemocidin 2 was thermostable (25–100 °C) and pH resistant (pH 3–10). The cellular integrity was determined by flow cytometry. AI-hemocidin 2 was capable of permeating the cellular membrane. Changes in the cell morphology were observed with a scanning electron microscope. Circular dichroism spectra suggested that AI-hemocidin 2 formed an α-helix structure in the membrane mimetic environment. The results indicated that the anti-bacterial mechanism for AI-hemocidin 2 occurred through disrupting the cell membrane. AI-hemocidin 2 might be a potential candidate for tackling antibiotic resistant bacteria. View Full-Text
Keywords: Arca inflata; peptide; hemoglobin; purification; structural elucidation; antibacterial activity Arca inflata; peptide; hemoglobin; purification; structural elucidation; antibacterial activity
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MDPI and ACS Style

Li, C.; Zhu, J.; Wang, Y.; Chen, Y.; Song, L.; Zheng, W.; Li, J.; Yu, R. Antibacterial Activity of AI-Hemocidin 2, a Novel N-Terminal Peptide of Hemoglobin Purified from Arca inflata. Mar. Drugs 2017, 15, 205.

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    Description: Figure S1. Purity Confirmation of J1S1. (A) the result of Tricine-SDS-PAGE; (B) the result of Native PAGE; (C) the result of RP-HPLC. Figure S2. The results of N-terminal amino acid sequencing of Hb-I.
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    Description: Graphic Abstract
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