0000000000582375

AUTHOR

Aleksandra Mikołajczyk

showing 2 related works from this author

Zn(II)-alloferon complexes - Similar sequence, different coordination modes, no antibacterial activity.

2020

Often, in the search for a highly defined scientific phenomenon, a different one becomes apparent. This was also the case of this work, in the scope of which we planned to search for metal-enhanced, novel antibacterial/ antifungal compounds. Instead, we denied the existence of such and revealed the details of the bioinorganic chemistry of Zn(II)-alloferon complexes. Zinc(II) complexes of alloferon 1 and 2, ligands with a sequential difference of one amino acid only, show a substantially different coordination pattern at physiological pH. In the case of Zn(II)-alloferon 1 species, a histamine-like binding mode is observed (N-terminal amine and imidazole of His-1) and the coordination sphere …

Coordination sphereAlloferon; Metal-antimicrobial peptide complex; Metal-peptide thermodynamics; Zinc(II)StereochemistryProton Magnetic Resonance Spectroscopychemistry.chemical_elementZincMicrobial Sensitivity Tests010402 general chemistryLigands01 natural sciencesBiochemistryMass SpectrometryInorganic ChemistryAlloferonchemistry.chemical_compoundStructure-Activity RelationshipCoordination ComplexesImidazoleMetal-antimicrobial peptide complexHistidineAmino Acid Sequencechemistry.chemical_classificationMetal-peptide thermodynamics010405 organic chemistryBioinorganic chemistryZinc(II)0104 chemical sciencesAmino acidAnti-Bacterial AgentsZincchemistryThermodynamicsChemical stabilityAmine gas treatingAntibacterial activityPeptidesJournal of inorganic biochemistry
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Zn-Enhanced Asp-Rich Antimicrobial Peptides N-Terminal Coordination by Zn(II) and Cu(II), Which Distinguishes Cu(II) Binding to Different Peptides

2021

The antimicrobial activity of surfactant-associated anionic peptides (SAAPs), which are isolated from the ovine pulmonary surfactant and are selective against the ovine pathogen Mannheimia haemolytica, is strongly enhanced in the presence of Zn(II) ions. Both calorimetry and ITC measurements show that the unique Asp-only peptide SAAP3 (DDDDDDD) and its analogs SAAP2 (GDDDDDD) and SAAP6 (GADDDDD) have a similar micromolar affinity for Zn(II), which binds to the N-terminal amine and Asp carboxylates in a net entropically-driven process. All three peptides also bind Cu(II) with a net entropically-driven process but with higher affinity than they bind Zn(II) and coordination that involves the N…

Pore Forming Cytotoxic Proteins0301 basic medicineStereochemistryQH301-705.5Metal ions in aqueous solutionAntimicrobial peptidesPeptide010402 general chemistry01 natural sciencesArticleCatalysisInorganic Chemistry03 medical and health scienceschemistry.chemical_compoundthermodynamicsDeprotonationZn(II) and Cu(II) bioinorganic chemistryPulmonary surfactantAmidePhysical and Theoretical ChemistryBiology (General)Mannheimia haemolyticaMolecular BiologyQD1-999Spectroscopychemistry.chemical_classificationOrganic ChemistryElectron Spin Resonance SpectroscopyGeneral Medicine0104 chemical sciencesComputer Science ApplicationsZincChemistry030104 developmental biologyMembranechemistryAmine gas treatingmetal-antimicrobial peptide interactionsPeptidesCopperInternational Journal of Molecular Sciences
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