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Special Issue "Cyclic Peptide Analogues and Non-Peptide Mimetics"

A special issue of Molecules (ISSN 1420-3049).

Deadline for manuscript submissions: 31 December 2020.

Special Issue Editor

Assoc. Prof. Dr. Theodore Tselios
Website
Guest Editor
Department of Chemistry, University of Patras, Patra, Greece
Interests: organic; peptide and medicinal chemistry; rational design and synthesis of linear; cyclic peptide analogues and non-peptide mimetics; conformational studies; molecular modelling of bioactive and pharmaceutical compounds; interactions of bioactive molecules (docking studies); pharmacophore analysis; homology modelling

Special Issue Information

Dear Colleagues,

It is a great pleasure and honour for me to ask for your contribution to a Special Issue related to cyclic peptides and non-peptide mimetics. This significant and timely topic inaugurates new opportunities in the design, discovery, and development of pharmaceutical products. Peptides and proteins are significant tools for drug development and are considered attractive "drug leads" for the rational design of bioactive molecules and molecules for medical use. The growing interest in peptide-based drugs in medicinal research provides many opportunities for the development of cyclic peptides and non-peptide mimetics aiming for the treatment of several diseases. Peptide cyclization and peptidomimetics restrict the conformational flexibility of their linear counterparts, and result in increased metabolic stability and receptor selectivity, therefore providing a better pharmacological profile. The knowledge of the bioactive conformation of linear peptides in combination with structure activity relations studies (SARs) are the main tools for the "structure-based design" and development of potent cyclic peptides and non-peptide mimetics.

The principal goal of this Special Issue is to provide the scientific community with novel approaches and directions in the field of rational drug design and medicinal chemistry, using cyclic peptides and non-peptide mimetics. I cordially invite researchers working in this field to join this Issue and submit original research articles, short communications, and review articles.

Assoc. Prof. Dr. Theodore Tselios
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. Molecules is an international peer-reviewed open access semimonthly 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 2000 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

  • Cyclic peptides
  • Peptidomimetics and non-peptide mimetics
  • Rational design of bioactive molecules
  • Bioactive cyclic peptides

Published Papers (3 papers)

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Research

Open AccessArticle
Convergent Synthesis of Thioether Containing Peptides
Molecules 2020, 25(1), 218; https://doi.org/10.3390/molecules25010218 - 05 Jan 2020
Abstract
Thioether containing peptides were obtained following three synthetic routes. In route A, halo acids esterified on 2-chlorotrityl(Cltr) resin were reacted with N-fluorenylmethoxycarbonyl (Fmoc) aminothiols. These were either cleaved from the resin to the corresponding (Fmoc-aminothiol)carboxylic acids, which were used as key building [...] Read more.
Thioether containing peptides were obtained following three synthetic routes. In route A, halo acids esterified on 2-chlorotrityl(Cltr) resin were reacted with N-fluorenylmethoxycarbonyl (Fmoc) aminothiols. These were either cleaved from the resin to the corresponding (Fmoc-aminothiol)carboxylic acids, which were used as key building blocks in solid phase peptide synthesis (SPPS), or the N-Fmoc group was deprotected and peptide chains were elongated by standard SPPS. The obtained N-Fmoc protected thioether containing peptides were then condensed either in solution, or on solid support, with the appropriate amino components of peptides. In route B, the thioether containing peptides were obtained by the reaction of N-Fmoc aminothiols with bromoacetylated peptides, which were synthesized on Cltr-resin, followed by removal of the N-Fmoc group and subsequent peptide elongation by standard SPPS. In route C, the thioether containing peptides were obtained by the condensation of a haloacylated peptide synthesized on Cltr-resin and a thiol-peptide synthesized either on 4-methoxytrityl(Mmt) or trityl(Trt) resin. Full article
(This article belongs to the Special Issue Cyclic Peptide Analogues and Non-Peptide Mimetics)
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Open AccessArticle
Solid-Phase Insertion of N-mercaptoalkylglycine Residues into Peptides
Molecules 2019, 24(23), 4261; https://doi.org/10.3390/molecules24234261 - 22 Nov 2019
Abstract
N-mercaptoalkylglycine residues were inserted into peptides by reacting N-free amino groups of peptides, which were initially synthesized on 2-chlorotrityl resin (Cltr) using the Fmoc/tBu method, with bromoacetic acid and subsequent nucleophilic replacement of the bromide by reacting with S [...] Read more.
N-mercaptoalkylglycine residues were inserted into peptides by reacting N-free amino groups of peptides, which were initially synthesized on 2-chlorotrityl resin (Cltr) using the Fmoc/tBu method, with bromoacetic acid and subsequent nucleophilic replacement of the bromide by reacting with S-4-methoxytrityl- (Mmt)/S-trityl- (Trt) protected aminothiols. The synthesized thiols containing peptide–peptoid hybrids were cleaved from the resin, either protected by treatment with dichloromethane (DCM)/trifluoroethanol (TFE)/acetic acid (AcOH) (7:2:1), or deprotected (fully or partially) by treatment with trifluoroacetic acid (TFA) solution using triethylsilane (TES) as a scavenger. Full article
(This article belongs to the Special Issue Cyclic Peptide Analogues and Non-Peptide Mimetics)
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Open AccessArticle
Conformation and Dynamics of the Cyclic Lipopeptide Viscosinamide at the Water-Lipid Interface
Molecules 2019, 24(12), 2257; https://doi.org/10.3390/molecules24122257 - 17 Jun 2019
Cited by 2
Abstract
Cyclic lipodepsipeptides or CLiPs from Pseudomonas are secondary metabolites that mediate a wide range of biological functions for their producers, and display antimicrobial and anticancer activities. Direct interaction of CLiPs with the cellular membranes is presumed to be essential in causing these. To [...] Read more.
Cyclic lipodepsipeptides or CLiPs from Pseudomonas are secondary metabolites that mediate a wide range of biological functions for their producers, and display antimicrobial and anticancer activities. Direct interaction of CLiPs with the cellular membranes is presumed to be essential in causing these. To understand the processes involved at the molecular level, knowledge of the conformation and dynamics of CLiPs at the water-lipid interface is required to guide the interpretation of biophysical investigations in model membrane systems. We used NMR and molecular dynamics to study the conformation, location and orientation of the Pseudomonas CLiP viscosinamide in a water/dodecylphosphocholine solution. In the process, we demonstrate the strong added value of combining uniform, isotope-enriched viscosinamide and protein NMR methods. In particular, the use of techniques to determine backbone dihedral angles and detect and identify long-lived hydrogen bonds, establishes that the solution conformation previously determined in acetonitrile is maintained in water/dodecylphosphocholine solution. Paramagnetic relaxation enhancements pinpoint viscosinamide near the water-lipid interface, with its orientation dictated by the amphipathic distribution of hydrophobic and hydrophilic residues. Finally, the experimental observations are supported by molecular dynamics simulations. Thus a firm structural basis is now available for interpreting biophysical and bioactivity data relating to this class of compounds. Full article
(This article belongs to the Special Issue Cyclic Peptide Analogues and Non-Peptide Mimetics)
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