Zn-Enhanced Asp-Rich Antimicrobial Peptides N-Terminal Coordination by Zn(II) and Cu(II), Which Distinguishes Cu(II) Binding to Different Peptides
| Autor: | Magdalena Rowińska-Żyrek, Joanna Wątły, Adriana Miller, Dean E. Wilcox, Danuta Witkowska, Agnieszka Matera-Witkiewicz, Aleksandra Mikołajczyk |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Pore Forming Cytotoxic Proteins
0301 basic medicine Stereochemistry QH301-705.5 Metal ions in aqueous solution Antimicrobial peptides Peptide 010402 general chemistry 01 natural sciences Article Catalysis Inorganic Chemistry 03 medical and health sciences chemistry.chemical_compound thermodynamics Deprotonation Zn(II) and Cu(II) bioinorganic chemistry Pulmonary surfactant Amide Physical and Theoretical Chemistry Biology (General) Mannheimia haemolytica Molecular Biology QD1-999 Spectroscopy chemistry.chemical_classification Organic Chemistry Electron Spin Resonance Spectroscopy General Medicine 0104 chemical sciences Computer Science Applications Zinc Chemistry 030104 developmental biology Membrane chemistry Amine gas treating metal-antimicrobial peptide interactions Peptides Copper |
| Zdroj: | International Journal of Molecular Sciences Volume 22 Issue 13 International Journal of Molecular Sciences, Vol 22, Iss 6971, p 6971 (2021) |
| ISSN: | 1422-0067 |
| DOI: | 10.3390/ijms22136971 |
| Popis: | 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-terminal amine and deprotonated amides as the pH increases. The parent SAAP3 binds Cu(II) with the highest affinity however, as shown with potentiometry and absorption, CD and EPR spectroscopy, Asp residues in the first and/or second positions distinguish Cu(II) binding to SAAP3 and SAAP2 from their binding to SAAP6, decreasing the Cu(II) Lewis acidity and suppressing its square planar amide coordination by two pH units. We also show that these metal ions do not stabilize a membrane disrupting ability nor do they induce the antimicrobial activity of these peptides against a panel of human pathogens. |
| Databáze: | OpenAIRE |
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