Special Issue "Toxic Non-Proteinogenic Amino Acids (NPAA)"

A special issue of Toxins (ISSN 2072-6651).

Deadline for manuscript submissions: closed (30 September 2017).

Special Issue Editor

Prof. Dr. John P. Berry
E-Mail Website
Guest Editor
Institute of Environment, Department of Chemistry and Biochemistry, Florida International University (FIU), 354 Marine Science, Biscayne Bay Campus, 3000 NE 151st St., North Miami, FL 33181, USA
Interests: cyanobacteria; toxins; bioactive compounds; zebrafish embryo model; natural products
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Special Issue Information

Dear Colleagues,

Amino acids are clearly key molecules in the chemistry of life, and indeed, are the most abundant biomolecules (constituting, for example, as much as 50% dry weight of biological systems in the form either proteins or free amino acids). By far, most attention has focused on the canonical twenty amino acids utilized in ribosomal protein synthesis via translation. However, it is generally accepted that the proteinogenic amino acids represent only a very small subset of the diversity of amino acids, and estimates suggest that several hundred or more non-proteinogenic amino acids (NPAAs) are produced and exist in nature. The NPAA are produced in the environment by a wide range of organisms including, in particular, various plant and microbial taxa. Reported functions of the NPAA include endogenous roles such as cellular signaling and regulation, structural composition of cell membranes and metabolic intermediates, as well as various “exogenous”, and particularly ecological, roles as feeding deterrents, and other allelopathic (e.g., antimicrobial or other antibiotic) activities. Notably, the NPAAs are found in a wide range of biologically active peptides from microbes. Alongside these roles, several examples exist to suggest that NPAAs may secondarily pose threats to human and animal health as potent toxins and/or contributors to diseases (e.g., neurodegenerative disease). These diverse functions, and reported impacts on health, point to a largely under-investigated contribution of NPAAs as natural toxins. This Special Issue will focus, therefore, on toxic amino acids including their diversity, biosynthesis/biogenesis, mechanisms of toxicity and possible roles in a wide range of biological processes including, in particular, human health and disease. Manuscripts from any fields, and disciplines, related to toxic amino acids are invited.

Prof. Dr. John P. Berry
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 double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.

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Published Papers (1 paper)

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Review

Review
Toxic Dimethylarginines: Asymmetric  Dimethylarginine (ADMA) and Symmetric  Dimethylarginine (SDMA)
Toxins 2017, 9(3), 92; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins9030092 - 06 Mar 2017
Cited by 102 | Viewed by 4830
Abstract
Asymmetric and symmetric dimethylarginine (ADMA and SDMA, respectively) are toxic, non‐proteinogenic amino acids formed by post‐translational modification and are uremic toxins that inhibit nitric oxide (NO) production and play multifunctional roles in many human diseases. Both ADMA and SDMA have emerged as strong [...] Read more.
Asymmetric and symmetric dimethylarginine (ADMA and SDMA, respectively) are toxic, non‐proteinogenic amino acids formed by post‐translational modification and are uremic toxins that inhibit nitric oxide (NO) production and play multifunctional roles in many human diseases. Both ADMA and SDMA have emerged as strong predictors of cardiovascular events and death in a range of illnesses. Major progress has been made in research on ADMA‐lowering therapies in animal studies; however, further studies are required to fill the translational gap between animal models and clinical trials in order to treat human diseases related to elevated ADMA/SDMA levels. Here, we review the reported impacts of ADMA and SDMA on human health and disease, focusing on the synthesis and metabolism of ADMA and SDMA; the pathophysiological roles of these dimethylarginines; clinical conditions and animal models associated with elevated ADMA and SDMA levels; and potential therapies against ADMA and SDMA. There is currently no specific pharmacological therapy for lowering the levels and counteracting the deleterious effects of ADMA and SDMA. A better understanding of the mechanisms underlying the impact of ADMA and SDMA on a wide range of human diseases is essential to the development of specific therapies against diseases related to ADMA and SDMA. Full article
(This article belongs to the Special Issue Toxic Non-Proteinogenic Amino Acids (NPAA))
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