A5030021102- Tuberculosis Research and Epidemiology
- Trace Elements in Health
- Mycobacterium research and diagnosis
- Protein Structure and Dynamics
- Minerals Flotation and Separation Techniques
- Mass Spectrometry Techniques and Applications
- Advanced Proteomics Techniques and Applications
- Adsorption and biosorption for pollutant removal
- Bacterial Genetics and Biotechnology
- Pneumocystis jirovecii pneumonia detection and treatment
- Plant Micronutrient Interactions and Effects
- Integrated Water Resources Management
- Antibiotic Resistance in Bacteria
- RNA and protein synthesis mechanisms
- Antifungal resistance and susceptibility
- History and advancements in chemistry
- Antimicrobial Resistance in Staphylococcus
- Analytical Chemistry and Chromatography
University of Wrocław
2020-2024
This study contrasts the Cu( ii )/Ni( )/Zn( ) complex stability of GroEL1 C-terminal domains: His-rich ABS ( M. abscessus and Glu/His-rich XEN xenopi ). forms more stable complexes, favoring histidine over glutamic acid for metal ion binding.
The mycobacterial histidine-rich GroEL1 protein differs significantly compared to the well-known methionine/glycine-rich GroEL chaperonin. It was predicted that can play a significant role in metal homeostasis of Mycobacteria but not, as its analogue, folding. In this paper, we present properties His-rich C-terminus ligand for Cu(II) ions. We studied stoichiometry, stability, and spectroscopic features copper complexes eight model peptides: L1─Ac-DHDHHHGHAH, L2─Ac-DKPAKAEDHDHHHGHAH, six...
High complexity of cell and tissue proteomes limits the investigation proteomic biomarkers. Therefore, methods enrichment some chemical groups peptides including thiopeptides are important tools that may facilitate analysis by reducing sample increasing proteome coverage. Here, we present a new method cysteine-containing tryptic peptide using commercially available TentaGel R RAM resin modified linker containing maleimide group, allowing thiol conjugation. The captured lysine residue were...
The increasing number of antibiotic-resistant pathogens has become one the foremost health problems modern times. One most lethal and multidrug-resistant bacteria is Mycobacterium tuberculosis (Mtb), which causes (TB). TB continues to engulf systems due significant development bacterial strains. Mammalian immune system response mycobacterial infection includes, but not limited to, concentration zinc(II) other divalent metal ions in phagosome vesicles up toxic levels. Metal are necessary for...
Recently, we have studied the coordination chemistry of Cu(II)-histidine-rich C-terminal tail (HRCT) complex mycobacterial GroEL1 protein. The structure this domain differs significantly compared to well-known methionine-glycine-rich GroEL chaperonin - it was predicted that could play a significant role in metal homeostasis
Infections caused by Candida species are becoming seriously dangerous and difficult to cure due their sophisticated mechanisms of resistance. The host organism defends itself from the invader, e.g., increasing concentration metal ions. Therefore, there is a need understand overall homeostasis in species. One them associated with AMT1, an important virulence factor derived glabrata, another MAC1, present albicans. Both proteins possess homologous Cys/His-rich domain. In our studies, we have...
The formation equilibria of zinc( ii ) complexes the α5 binding domain SmtB/BigR4 proteins and mutants latter are studied an unusual behaviour histidine ligands is observed.
In the Biological Inorganic Chemistry Group we are inspired to better understand metal ions acquisition and homeostasis in pathogenic bacteria, this review present three different approaches role of these processes. The growing importance a full understanding iron transport system pathogens prompted us study synthetic analogs siderophores, used as structural probes process uptake by microorganisms. ferrichrome biomimetic allowed efficient Fe(III) chelation under biological conditions were...