Metal–Peptide Complexes with Antimicrobial Potential for Cotton Fiber Protection
A study of the formation of copper (II) complexes with hemorphin peptide motifs in alkalic water solutions is presented. The effect of the peptide ligand on the complexing properties of the Cu (II) ion was quantified by giving the stoichiometry and stability of the complex compounds in the medium in...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-02-01
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| Series: | Journal of Functional Biomaterials |
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| Online Access: | https://www.mdpi.com/2079-4983/14/2/106 |
| _version_ | 1797620104420130816 |
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| author | Stela Georgieva Petar Todorov Desislava Staneva Petar Grozdanov Ivanka Nikolova Ivo Grabchev |
| author_facet | Stela Georgieva Petar Todorov Desislava Staneva Petar Grozdanov Ivanka Nikolova Ivo Grabchev |
| author_sort | Stela Georgieva |
| collection | DOAJ |
| description | A study of the formation of copper (II) complexes with hemorphin peptide motifs in alkalic water solutions is presented. The effect of the peptide ligand on the complexing properties of the Cu (II) ion was quantified by giving the stoichiometry and stability of the complex compounds in the medium in which they are formed using voltammetric (cyclic) and spectral (UV-Vis and fluorimetric) analytical techniques. The resulting complexes were examined via IR spectroscopy to detect M-N and M-O oscillations and using the EPR approach in solution and in the solid phase to view the coordination and ligand binding regime. The possibility of the synergistic action of copper ions in the antivirus protection processes of cotton fibers coated in the same solvent with the newly obtained complex compounds was also investigated. One of the advantages is the formation of the complexes in an environment where the immobilization takes place, which contributes to increasing the efficiency of the process. The obtained results may serve as an aid for future more detailed biological studies of structure–activity relationships (SARs). |
| first_indexed | 2024-03-11T08:36:23Z |
| format | Article |
| id | doaj.art-243812aeb92a4c31ad2edc36407352ba |
| institution | Directory Open Access Journal |
| issn | 2079-4983 |
| language | English |
| last_indexed | 2024-03-11T08:36:23Z |
| publishDate | 2023-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Journal of Functional Biomaterials |
| spelling | doaj.art-243812aeb92a4c31ad2edc36407352ba2023-11-16T21:24:44ZengMDPI AGJournal of Functional Biomaterials2079-49832023-02-0114210610.3390/jfb14020106Metal–Peptide Complexes with Antimicrobial Potential for Cotton Fiber ProtectionStela Georgieva0Petar Todorov1Desislava Staneva2Petar Grozdanov3Ivanka Nikolova4Ivo Grabchev5Department of Analytical Chemistry, University of Chemical Technology and Metallurgy, 1756 Sofia, BulgariaDepartment of Organic Chemistry, University of Chemical Technology and Metallurgy, 1756 Sofia, BulgariaDepartment of Textile, Leathers and Fuels, University of Chemical Technology and Metallurgy, 1756 Sofia, BulgariaThe Stephan Angeloff Institute of Microbiology, Bulgarian Academy of Sciences, 1113 Sofia, BulgariaThe Stephan Angeloff Institute of Microbiology, Bulgarian Academy of Sciences, 1113 Sofia, BulgariaFaculty of Medicine, Sofia University “St. Kl. Ohridski”, 1407 Sofia, BulgariaA study of the formation of copper (II) complexes with hemorphin peptide motifs in alkalic water solutions is presented. The effect of the peptide ligand on the complexing properties of the Cu (II) ion was quantified by giving the stoichiometry and stability of the complex compounds in the medium in which they are formed using voltammetric (cyclic) and spectral (UV-Vis and fluorimetric) analytical techniques. The resulting complexes were examined via IR spectroscopy to detect M-N and M-O oscillations and using the EPR approach in solution and in the solid phase to view the coordination and ligand binding regime. The possibility of the synergistic action of copper ions in the antivirus protection processes of cotton fibers coated in the same solvent with the newly obtained complex compounds was also investigated. One of the advantages is the formation of the complexes in an environment where the immobilization takes place, which contributes to increasing the efficiency of the process. The obtained results may serve as an aid for future more detailed biological studies of structure–activity relationships (SARs).https://www.mdpi.com/2079-4983/14/2/106peptidehemorphincopper–peptide complexesCu(II) ionscottonantivirus protection |
| spellingShingle | Stela Georgieva Petar Todorov Desislava Staneva Petar Grozdanov Ivanka Nikolova Ivo Grabchev Metal–Peptide Complexes with Antimicrobial Potential for Cotton Fiber Protection Journal of Functional Biomaterials peptide hemorphin copper–peptide complexes Cu(II) ions cotton antivirus protection |
| title | Metal–Peptide Complexes with Antimicrobial Potential for Cotton Fiber Protection |
| title_full | Metal–Peptide Complexes with Antimicrobial Potential for Cotton Fiber Protection |
| title_fullStr | Metal–Peptide Complexes with Antimicrobial Potential for Cotton Fiber Protection |
| title_full_unstemmed | Metal–Peptide Complexes with Antimicrobial Potential for Cotton Fiber Protection |
| title_short | Metal–Peptide Complexes with Antimicrobial Potential for Cotton Fiber Protection |
| title_sort | metal peptide complexes with antimicrobial potential for cotton fiber protection |
| topic | peptide hemorphin copper–peptide complexes Cu(II) ions cotton antivirus protection |
| url | https://www.mdpi.com/2079-4983/14/2/106 |
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