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Special Issue "Marine Drugs Interact with Functional Proteins"

A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: 31 May 2018

Special Issue Editor

Guest Editor
Prof. Masaki Kita

Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan
Website | E-Mail
Interests: Natural products; Biologically and physiologically intriguing phenomena; Spectoscopic analysis; Target identification; Mode of action

Special Issue Information

Dear Colleagues,

It has been shown that a number of marine natural products interact with functional proteins to show potent biological and physiological activities. For example, an anticancer drug, eribulin, derived from the marine macrolide halichondrin B, is a unique inhibitor of microtubule dynamics. Some marine natural products have recently been shown to induce or inhibit protein‒protein interactions. These new mechanistic findings should be useful for the design and development of new pharmacological tools and therapeutic agents.

This Special Issue will highlight the progress in the following topics: Isolation and structures of bioactive marine natural products (such as anti-tumor, anti-bacterial, anti-inflammation, anti-oxidant compounds) that target functional proteins; development and use of chemical probes inspired from bioactive marine natural products; target protein identification and mechanism of action studies; structural and kinetic analysis of protein–ligand interactions; and structure-activity relationship studies and drug discovery study of marine bioactive compounds that interfere in protein dynamics.

Prof. Masaki Kita
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Marine Drugs is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Marine natural products
  • Bioactive secondary metabolites
  • Target protein identification
  • Mechanism of action
  • Interference toward protein dynamics including protein–protein interaction
  • Structural and kinetic analysis of protein–ligand interactions
  • Structure-activity relationships
  • Drug discovery

Published Papers (1 paper)

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Research

Open AccessArticle Functional Expression and Characterization of the Recombinant N-Acetyl-Glucosamine/N-Acetyl-Galactosamine-Specific Marine Algal Lectin BPL3
Mar. Drugs 2018, 16(1), 13; doi:10.3390/md16010013
Received: 28 November 2017 / Revised: 16 December 2017 / Accepted: 28 December 2017 / Published: 5 January 2018
PDF Full-text (2140 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Lectins, characterized by their carbohydrate-binding ability, have extensive practical applications. However, their industrial use is limited due to impurity. Thus, quality-controlled production of recombinant lectin is necessary. In this study, the algal lectin BPL3 (Bryopsis plumosa lectin 3) was successfully produced using
[...] Read more.
Lectins, characterized by their carbohydrate-binding ability, have extensive practical applications. However, their industrial use is limited due to impurity. Thus, quality-controlled production of recombinant lectin is necessary. In this study, the algal lectin BPL3 (Bryopsis plumosa lectin 3) was successfully produced using a bacterial expression system, BL21(DE3), with an artificial repeated structure (dimeric construct). Recombinant dimeric BPL3 (rD2BPL3) was confirmed by LC-MS/MS spectrometry. Expression efficiency was greater for the construct with the repeat structure (rD2BPL3) than the monomeric form (rD1BPL3). Optimal conditions for expression were 1 mM IPTG at 20 °C. Recombinant lectin was purified under denaturing conditions and refolded by the flash dilution method. Recombinant BPL3 was solubilized in 1× PBS containing 2 M urea. rD2BPL3 showed strong hemagglutination activity using human erythrocyte. rD2BPL3 had a similar sugar specificity to that of the native protein, i.e., to N-acetyl-glucosamine (GlcNAc) and N-acetyl-galactosamine (GalNAc). Glycan array results showed that recombinant BPL3 and native BPL3 exhibited different binding properties. Both showed weak binding activity to α-Man-Sp. Native BPL3 showed strong binding specificity to the alpha conformation of amino sugars, and rD2BPL3 had binding activity to the beta conformation. The process developed in this study was suitable for the quality-controlled large-scale production of recombinant lectins. Full article
(This article belongs to the Special Issue Marine Drugs Interact with Functional Proteins)
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