Next Article in Journal
Tricholides A and B and Unnarmicin D: New Hybrid PKS-NRPS Macrocycles Isolated from an Environmental Collection of Trichodesmium thiebautii
Next Article in Special Issue
Two Furanosesterterpenoids from the Sponge Luffariella variabilis
Previous Article in Journal
Isobenzofuranones and Isochromenones from the Deep-Sea Derived Fungus Leptosphaeria sp. SCSIO 41005
Previous Article in Special Issue
Biscembranoids and Cembranoids from the Soft Coral Sarcophyton elegans
Article Menu
Issue 7 (July) cover image

Export Article

Open AccessArticle
Mar. Drugs 2017, 15(7), 205; doi:10.3390/md15070205

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
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
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)
View Full-Text   |   Download PDF [2172 KB, uploaded 30 June 2017]   |  

Abstract

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
Figures

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary materials

  • Supplementary File 1:

    Supplementary (PDF, 305 KB)

  • Externally hosted supplementary file 1
    Doi: no
    Link: http://no
    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.
  • Externally hosted supplementary file 2
    Doi: no
    Link: http://no
    Description: Graphic Abstract

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

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.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Mar. Drugs EISSN 1660-3397 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top