- Trace Elements in Health
- Metal complexes synthesis and properties
- Pneumocystis jirovecii pneumonia detection and treatment
- Protein Structure and Dynamics
- Bacterial Genetics and Biotechnology
- Peptidase Inhibition and Analysis
- Molecular Sensors and Ion Detection
- Antibiotic Resistance in Bacteria
- Mycobacterium research and diagnosis
- Tuberculosis Research and Epidemiology
- RNA and protein synthesis mechanisms
- Protein Interaction Studies and Fluorescence Analysis
- Antimicrobial Resistance in Staphylococcus
- Hemoglobin structure and function
- Biochemical and Structural Characterization
- Heavy Metal Exposure and Toxicity
- Drug Transport and Resistance Mechanisms
- Corrosion Behavior and Inhibition
- Plant Micronutrient Interactions and Effects
- Enzyme Structure and Function
- Venomous Animal Envenomation and Studies
- Lipid Membrane Structure and Behavior
- Prion Diseases and Protein Misfolding
- Boron Compounds in Chemistry
- Pesticide Exposure and Toxicity
University of Wrocław
2016-2025
Faculty (United Kingdom)
2015-2025
Laboratoire de Physique des 2 Infinis Irène Joliot-Curie
2018
Wroclaw University of Applied Informatics "Horizon"
2015
This review is focused on the general mechanisms of metal toxicity in humans. The possible and mainly confirmed their action are discussed. metals divided into four groups due to toxic effects. First group comprises ions acting as Fenton reaction catalyst iron copper. These types participate generation reactive oxygen species. Metals such nickel, cadmium chromium considered carcinogenic agents. Aluminum, lead tin involved neurotoxicity. representative last mercury, which may be a generally...
In chemistry, nature-inspired solutions are often the most trivial and effective ones. Histidine rich sequences used commercially in immobilized metal affinity chromatography (IMAC) as molecular 'anchors' that bind to a ion (usually nickel), by chelation with nitrilotriacetic acid (NTA) bound solid support. The typical (His)6 tag, present at C- or N-terminus of protein which is meant be purified, has been successfully for decades. Consecutive histidines common denominator both His-tags...
Often necessary for efficient Fe(II) trafficking into bacterial cell, the Feo system is a vital transporter many pathogenic bacteria and indispensable proper development survival in host organism during infection. In this work, we present metal-binding characteristics of peptidic models two putative Fe(II)-binding sites E. coliFeoB: L1 (Ac-477IMRGEATPFVMELPVYHVPH496-CONH2) being fragment Core CFeoB region located between transmembrane helices L2 (Ac-38VERKEG43-CONH2), which represents ExxE...
The coordination modes and thermodynamic stabilities of the complexes cysteine-rich N-terminal domain fragment ZIP13 zinc transporter (MPGCPCPGCG-NH(2)) with Zn(2+), Cd(2+), Bi(3+), Ni(2+) have been studied by potentiometric, mass spectrometric, NMR, CD, UV-vis spectroscopic methods. All metals had similar binding modes, three thiol sulfurs cysteine residues involved in metal ion coordination. stability formed solution changes series Bi(3+) ≫ Cd(2+) > Zn(2+) Ni(2+), strongest being for...
The histidine-rich sequence from the loop between tansmembrane domains (TMDs) III and IV of ZIP transporters binds all studied metal ions with different geometries stability increasing in series Ni<sup>2+</sup> < Zn<sup>2+</sup> ≪ Cu<sup>2+</sup>; a high specificity for is observed.
The FQH431SNLKQMSEFSVFLSLRNLIYLDISH456TH458TR fragment, containing three histidine residues, the conserved H431 and non-conserved H456 H458, located from 429 to 460 amino acid residues in C-terminal portion of human Toll-like-receptor 4 (hTLR4), which is directly activated by nickel, a well known contact allergen, has been tested for Ni(II) binding. complex formation capability 32-amino sequence with ions followed potentiometric, UV-Vis, CD, MS NMR measurements. able bind all histidines...
Copper complexes of a poly-His/poly-Gly peptide (EDDHHHHHHHHHGVGGGGGGGGGG-NH2), natural component snake venom, were studied by means both experimental (thermodynamic, spectroscopic and MS) techniques molecular dynamics (MD) simulations density functional theory (DFT) calculations. This proved to be an exceptionally effective copper chelator, forming which are thermodynamically more stable than those formed the albumin-like ATCUN motif several other poly-histidine protein fragments. We show...
The coordination properties of three peptides with CXXC motif: Ac-GCASCDNCRACKK-NH2, Ac-GCASCDNCRAAKK-NH2 and Ac-GCASCDNARAAKK-NH2 as donors four, two thiol ligands for Ni2+,Cd2+, Zn2+ Bi3+ were studied by potentiometric titrations, UV-Vis CD spectra measurements. Since the stability complexes is closely connected amount metal- bound cysteine sulfurs, competition plots 2, 3 4 cysteines further prove involvement all thiols in metal ion binding. Furthermore, sulfur- zinc appear to be much more...
HypA, a nickel accessory protein from H. pylori, binds zinc ion in it's structural site, loop with two conserved CXXC motifs (Ac-ELECKDCSHVFKPNALDYGVCEKCHS-NH(2)). There are at least three hypotheses on the binding mode of this ion. In paper, we try to understand how Zn(2+) fragment and why Ni(2+), metal quite high affinity towards thiolic sites, doesn't compete motif. Potentiometric titrations, mass spectrometry, NMR, UV-Vis CD spectroscopy help us compare coordination modes both complexes...
Iron(<sc>ii</sc>) clathrochelates are protein-sensitive CD reporters able to discriminate proteins of similar structure (HSA and BSA) reflect the transitions protein conformation.
The interactions between two peptide ligands [Ac763CCAASTTGDCH773 (P1) and Ac743RRARSRVDIELLATRKSVSSCCAASTTGDCH773 (P2)] derived from the cytoplasmic C-terminal region of Eschericha coli FeoB protein Fe(II), Mn(II), Zn(II) ions were investigated. Feo system is regarded as most important bacterial Fe(II) acquisition system, being one key virulence factors, especially in anaerobic conditions. Located inner membrane Gram-negative bacteria, transports periplasm to cytoplasm. Despite its crucial...
Recognition of elements protein tertiary structure is crucial for biotechnological and biomedical tasks; this makes the development optical sensors certain surface important. Herein, we demonstrated ability iron(II) clathrochelates (1-3) functionalized with mono-, di- hexa-carboxyalkylsulfide to induce selective circular dichroism (CD) response upon binding globular proteins. Thus, inherently CD-silent revealed inducing CD spectra when human serum albumin (HSA) (1, 2), beta-lactoglobuline...
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 role of the residues in hypa loop on stability its complexes with Zn<sup>2+</sup>, Cd<sup>2+</sup>and Ni<sup>2+</sup>ions.
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...
Soft metal ion binding enforces critical rearrangement of the structure Bri2-23, a natural inhibitor Aβ aggregation, thus shifting its solution behavior to self aggregating system.