Polypeptides and Bioconjugates: Synthesis, Anticancer and/or Antimicrobial Activities

A special issue of Pharmaceutics (ISSN 1999-4923). This special issue belongs to the section "Biologics and Biosimilars".

Deadline for manuscript submissions: 30 April 2024 | Viewed by 1075

Special Issue Editors


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Guest Editor
Biotechnology Department, University of Chemical Technology and Metallurgy, 8 Kliment Ohridski Blvd., 1756 Sofia, Bulgaria
Interests: biologically active peptides; bioconjugates; the development of new methods for the determination of organic compounds in different matrices

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Guest Editor
Department of Organic Chemistry, University of Chemical Technology and Metallurgy, 8 Kliment Ohridski Blvd, 1756 Sofia, Bulgaria
Interests: biologically active peptides; unnatural amino acids; organic chemistry; synthesis and study of biologically active peptides

Special Issue Information

Dear Colleagues,

Many medicines on the pharmaceutical market are based on peptides or modified amino acids, such as enalapril (Vasotec), acetylcysteine (chemical name N-acetyl-L-cysteine), peptide antibiotics, as well as several analogues of the peptide hormone somatostatin, named octreotide, lanreotide, and vapreotide, which is used to fight different types of cancer. Therefore, peptides have been well proven as possible alternatives for other medical drugs in the treatment of different illnesses.

In recent years, many scientific groups have worked on the synthesis of bioconjugates between peptides and other chemical structures in their efforts to identify molecules with synergistic effects and improved pharmacodynamics.

Thus, this Special Issue aims to highlight and unite the scientific studies of different groups and the contemporary progress in the field of new peptide-based structures with anticancer and/or antimicrobial activities. Mathematical predictions may also be included, as well as investigations into prodrugs based on amino acids.

Prof. Dr. Dancho Danalev
Prof. Dr. Emilia Naydenova
Guest Editors

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Keywords

  • peptides and bioconjugates with anticancer activity
  • peptides and bioconjugates with antimicrobial activity
  • peptides and bioconjugates with both anticancer and antimicrobial activity
  • prodrugs based on amino acids and peptides
  • mathematical modeling and prediction of properties of peptide molecules with anticancer/antimicrobial properties

Published Papers (1 paper)

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Research

19 pages, 8369 KiB  
Article
Interaction of KLAKLAK-NH2 and Analogs with Biomimetic Membrane Models
by Victoria Vitkova, Krassimira Antonova, Ognyan Petkov, Angelina Stoyanova-Ivanova, Sirine Jaber, Vladislava Ivanova, Emilia Naydenova and Dancho Danalev
Pharmaceutics 2024, 16(3), 340; https://doi.org/10.3390/pharmaceutics16030340 - 28 Feb 2024
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Abstract
Background: Specifically designed peptide mimetics offer higher selectivity regarding their toxicity to mammalian cells. In addition to the α-helix conformation, the specific activity is related to the peptide’s ability to penetrate the cell membrane. The alterations in lipid membrane properties were addressed in [...] Read more.
Background: Specifically designed peptide mimetics offer higher selectivity regarding their toxicity to mammalian cells. In addition to the α-helix conformation, the specific activity is related to the peptide’s ability to penetrate the cell membrane. The alterations in lipid membrane properties were addressed in the presence of the peptide KLAKLAK-NH2 and analogs containing β-alanine, strengthening the antibacterial activity and/or naphtalimide with proven anticancer properties. Methods: The molecular interactions of the peptide mimetics with POPC bilayers were studied using FTIR-ATR spectroscopy. The thermal shape fluctuation analysis of quasispherical unilamellar vesicles was applied to probe the membrane bending elasticity. The impedance characteristics of bilayer lipid membranes were measured using fast Fourier-transform electrochemical impedance spectroscopy. Results: A lateral peptide association with the membrane is reported for β-alanine-containing peptides. The most pronounced membrane softening is found for the NphtG-KLβAKLβAK-NH2 analog containing both active groups that corroborate with the indications for 1,8-naphthalimide penetration in the lipid hydrophobic area obtained from the FTIR-ATR spectra analysis. The β-alanine substitution induces strong membrane-rigidifying properties even at very low concentrations of both β-alanine-containing peptides. Conclusions: The reported results are expected to advance the progress in tailoring the pharmacokinetic properties of antimicrobial peptides with strengthened stability towards enzymatic degradation. The investigation of the nonspecific interactions of peptides with model lipid membranes is featured as a useful tool to assess the antitumor and antimicrobial potential of new peptide mimetics. Full article
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