Sławomir Potocki

ORCID: 0000-0002-5528-7200
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About
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Research Areas
  • 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...

10.2174/0929867321666140716093838 article EN Current Medicinal Chemistry 2014-07-15

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...

10.1039/c2nj40558j article EN New Journal of Chemistry 2012-10-26

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...

10.1021/acs.inorgchem.4c05111 article EN cc-by Inorganic Chemistry 2025-03-06

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...

10.1021/ic200270p article EN Inorganic Chemistry 2011-06-01

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> &lt; Zn<sup>2+</sup> ≪ Cu<sup>2+</sup>; a high specificity for is observed.

10.1039/c4dt00903g article EN Dalton Transactions 2014-01-01

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...

10.1039/c3dt52187g article EN Dalton Transactions 2013-10-09

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...

10.1039/c4dt02257b article EN Dalton Transactions 2014-09-10

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...

10.1039/c1dt10562k article EN Dalton Transactions 2011-01-01

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...

10.1039/c2dt32195e article EN Dalton Transactions 2012-12-11

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.

10.1039/c8mt00278a article EN cc-by Metallomics 2018-12-05

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...

10.1021/acs.inorgchem.3c02910 article EN cc-by Inorganic Chemistry 2023-11-01

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...

10.3390/biom10121602 article EN cc-by Biomolecules 2020-11-26

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.

10.1039/d3dt03579d article EN Dalton Transactions 2024-01-01

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.

10.1039/c5dt01005e article EN Dalton Transactions 2015-01-01

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...

10.1021/acs.inorgchem.2c04486 article EN cc-by Inorganic Chemistry 2023-04-24

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.

10.1039/c4mt00274a article EN Metallomics 2015-01-01
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