6533b853fe1ef96bd12ac100
RESEARCH PRODUCT
Zn-Enhanced Asp-Rich Antimicrobial Peptides N-Terminal Coordination by Zn(II) and Cu(II), Which Distinguishes Cu(II) Binding to Different Peptides
Magdalena Rowinska-zyrekJoanna WątłyAdriana MillerDean E. WilcoxDanuta WitkowskaAgnieszka Matera-witkiewiczAleksandra Mikołajczyksubject
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 interactionsPeptidesCopperdescription
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
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2021-06-28 | International Journal of Molecular Sciences |