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Special Issue "Marine Peptides"

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

Deadline for manuscript submissions: closed (30 April 2010)

Special Issue Editor

Guest Editor
Prof. Dr. Frank Mari

Department of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, Florida, USA
Website | E-Mail
Phone: +15612973315
Fax: +1 561 297 2759

Special Issue Information

Dear Colleagues,

The marine environment is a vast source of natural products. The biodiversity found in the oceans is remarkable and it has only begun to be explored recently, when compared with terrestrial habitats. The molecular variety associated with this biodiversity represents a challenge for drug discovery. Nevertheless, screening and pharmacological evaluation of marine natural products as potential drug leads has taken a giant leap in the past two decades. As a result, the first drug of marine origin has obtained approval by the FDA on December 31st 2004. Prialt, a peptide (an ω-conotoxin) isolated from a cone snail (Conus magus), has been approved for the treatment of chronic pain as a morphine replacement therapy and it is the most powerful painkiller known to date. This landmark event is evidence that a new wave of “Drugs from the Sea” with novel pharmacologies for the treatment of an array of diseases and conditions is on its way. This issue of Marine Drugs is dedicated to “Marine Peptides”. Whether these compounds are ribosomally-expressed, such as the conotoxins and sea anemone toxins, or enzymatically-produced peptides, they are of great interest as drug leads and for drug development. We hope that the manuscripts here included will cover several aspects of recent developments within the field.

Prof. Dr. Frank Mari
Guest Editor

Keywords

  • peptidic natural products
  • ribosomally-expressed
  • enzymatically-produced
  • cone snails
  • sea anemones
  • sponges
  • structure-activity
  • bioactivity
  • structural determination
  • bioavailability
  • peptide synthesis

Published Papers (2 papers)

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Research

Open AccessArticle Toward the Synthesis and Biological Screening of a Cyclotetrapeptide from Marine Bacteria
Mar. Drugs 2011, 9(1), 71-81; doi:10.3390/md9010071
Received: 11 November 2010 / Revised: 16 December 2010 / Accepted: 23 December 2010 / Published: 30 December 2010
Cited by 9 | PDF Full-text (223 KB) | HTML Full-text | XML Full-text
Abstract
The first synthesis of a naturally occurring tetrapeptide cyclo-(isoleucyl-prolyl-leucyl-alanyl) has been achieved using a solution-phase technique via coupling of dipeptide segments Boc-l-Pro-l-Leu-OH and l-Ala-l-Ile-OMe. Deprotection of the linear tetrapeptide unit and its subsequent cyclization gave a cyclopeptide, identical in all aspects to
[...] Read more.
The first synthesis of a naturally occurring tetrapeptide cyclo-(isoleucyl-prolyl-leucyl-alanyl) has been achieved using a solution-phase technique via coupling of dipeptide segments Boc-l-Pro-l-Leu-OH and l-Ala-l-Ile-OMe. Deprotection of the linear tetrapeptide unit and its subsequent cyclization gave a cyclopeptide, identical in all aspects to the naturally occurring compound. Bioactivity results indicated the antifungal and antihelmintic potential of the synthesized peptide against pathogenic dermatophytes and earthworms. Full article
(This article belongs to the Special Issue Marine Peptides)
Figures

Open AccessArticle In-Depth Analysis of Exoproteomes from Marine Bacteria by Shotgun Liquid Chromatography-Tandem Mass Spectrometry: the Ruegeria pomeroyi DSS-3 Case-Study
Mar. Drugs 2010, 8(8), 2223-2239; doi:10.3390/md8082223
Received: 7 June 2010 / Revised: 27 July 2010 / Accepted: 28 July 2010 / Published: 29 July 2010
Cited by 22 | PDF Full-text (318 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Microorganisms secrete into their extracellular environment numerous compounds that are required for their survival. Many of these compounds could be of great interest for biotechnology applications and their genes used in synthetic biology design. The secreted proteins and the components of the translocation
[...] Read more.
Microorganisms secrete into their extracellular environment numerous compounds that are required for their survival. Many of these compounds could be of great interest for biotechnology applications and their genes used in synthetic biology design. The secreted proteins and the components of the translocation systems themselves can be scrutinized in-depth by the most recent proteomic tools. While the secretomes of pathogens are well-documented, those of non-pathogens remain largely to be established. Here, we present the analysis of the exoproteome from the marine bacterium Ruegeria pomeroyi DSS-3 grown in standard laboratory conditions. We used a shotgun approach consisting of trypsin digestion of the exoproteome, and identification of the resulting peptides by liquid chromatography coupled to tandem mass spectrometry. Three different proteins that have domains homologous to those observed in RTX toxins were uncovered and were semi-quantified as the most abundantly secreted proteins. One of these proteins clearly stands out from the catalogue, representing over half of the total exoproteome. We also listed many soluble proteins related to ABC and TRAP transporters implied in the uptake of nutrients. The Ruegeria pomeroyi DSS-3 case-study illustrates the power of the shotgun nano-LC-MS/MS strategy to decipher the exoproteome from marine bacteria and to contribute to environmental proteomics. Full article
(This article belongs to the Special Issue Marine Peptides)

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