Metal–Peptide Complexes with Antimicrobial Potential for Cotton Fiber Protection

Abstract

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).

Sonication-Induced Boladipeptide-Based Metallogel as an Efficient Electrocatalyst for the Oxygen Evolution Reaction

“…Furthermore, Job’s plot was conducted to investigate the stoichiometry of the newly formed metallo-hydrogel. The graph shown in Figure S3, monitored at λ abs = 255 nm, indicates a binding ratio of 3:2 between boladipeptide and Ni 2+ . , Furthermore, the self-assembly and secondary structures of PBFY and Ni-PBFY-3 were examined by using the circular dichroism (CD) spectroscopic method. The CD spectra (Figure S4) of PBFY and Ni-PBFY-3 show positive peaks at 220 and 218 nm, and negative peaks at 231 and 230 nm, respectively.…”

Synthesis and Biological Activities of Some Metal Complexes of Peptides: A Review

“…Notably, the virucidal activity against human respiratory syncytial virus and adenovirus (HRSV-2) at 30 and 60 min remains weakly affected by these complexes, similar to the starting peptide compounds [56]. Recently, Georgieva et al proposed the formation of complexes between Cu(II) and hemorphin peptide derivatives in an aqueous solution with a pH of 10.98 [56]. Through meticulous examination of spectroscopic data and voltametric calculations, complete agreement has been reached, confirming the formation of stable copper(II) complexes with peptides in aqueous solutions.…”

“… Schematic structure of Cu(II)-peptide complexes Cu-C-V(L1), Cu-H-V(L2), Cu-AC-V (L3), Cu-AH-V (L4), and Cu-NCH7 (L6) Reprinted/adapted with permission from Ref. [ 56 ]. 2023, Georgieva et al [ 56 ].…”

“…Recently, Georgieva et al proposed the formation of complexes between Cu(II) and hemorphin peptide derivatives in an aqueous solution with a pH of 10.98 [ 56 ]. Through meticulous examination of spectroscopic data and voltametric calculations, complete agreement has been reached, confirming the formation of stable copper(II) complexes with peptides in aqueous solutions.…”

“…These complexes exhibit a 1:2 stoichiometry for Cu-H-V, Cu-AH-V, Cu-NH7C, and Cu-NCH7, while a 1:1 stoichiometry is observed for Cu-AC-V and Cu-C-V. Notably, the virucidal activity against human respiratory syncytial virus and adenovirus (HRSV-2) at 30 and 60 min remains weakly affected by these complexes, similar to the starting peptide compounds [ 56 ]. Figure 11 illustrates the structures of two of these newly identified complexes.…”