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  1. Artikel ; Online: Investigation of metal interactions with YrpE protein of Bacillus subtilis by a polyhistidine peptide model

    Bellotti, Denise / Leveraro, Silvia / Hecel, Aleksandra / Remelli, Maurizio

    Analytical Biochemistry. 2023 Nov., v. 680 p.115315-

    2023  

    Abstract: The use of model peptides that can simulate the behaviour of a protein domain is a very successful analytical method to study the metal coordination sites in biological systems. Here we study zinc and copper binding ability of the sequence HTHEHSHDHSHAH, ...

    Abstract The use of model peptides that can simulate the behaviour of a protein domain is a very successful analytical method to study the metal coordination sites in biological systems. Here we study zinc and copper binding ability of the sequence HTHEHSHDHSHAH, which serves as model for the metal interactions with YrpE, a putative metal-binding protein of the ZinT family identified in Bacillus subtilis. Compared to other ZinT proteins secreted by Gram-negative bacteria, the metal-coordination properties of YrpE N-terminal histidine-rich domain have not been yet characterized. Different independent analytical methods, aimed at providing information on the stability and structure of the formed species, have been employed, including potentiometric titrations, electrospray ionization mass spectrometry, UV–Vis spectrophotometry, circular dichroism and electron paramagnetic resonance spectroscopy. The obtained speciation models and equilibrium constants allowed to compare the metal-binding ability of the investigated polyhistidine sequence with that of other well-known histidine-rich peptides. Our thermodynamic results revealed that the YrpE domain HTHEHSHDHSHAH forms more stable metal complexes than other His-rich domains of similar ZinT proteins. Moreover, the studied peptide, containing the alternated (-XH-)ₙ motif, proved to be even more effective than the His6-tag (widely used in immobilized metal ion affinity chromatography) in binding zinc ions.
    Schlagwörter Bacillus subtilis ; affinity chromatography ; circular dichroism spectroscopy ; electron paramagnetic resonance spectroscopy ; electrospray ionization mass spectrometry ; models ; peptides ; protein domains ; thermodynamics ; zinc ; Metal-protein interaction ; Peptide models ; Polyhistidine tag ; Analytical methods ; Solution equilibria
    Sprache Englisch
    Erscheinungsverlauf 2023-11
    Erscheinungsort Elsevier Inc.
    Dokumenttyp Artikel ; Online
    ZDB-ID 1110-1
    ISSN 1096-0309 ; 0003-2697
    ISSN (online) 1096-0309
    ISSN 0003-2697
    DOI 10.1016/j.ab.2023.115315
    Datenquelle NAL Katalog (AGRICOLA)

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  2. Artikel ; Online: Metal-protein solution interactions investigated using model systems: Thermodynamic and spectroscopic methods.

    Bellotti, Denise / Leveraro, Silvia / Remelli, Maurizio

    Methods in enzymology

    2023  Band 687, Seite(n) 279–341

    Abstract: The first-row D-block metal ions are essential for the physiology of living organisms, functioning as cofactors in metalloproteins or structural components for enzymes: almost half of all proteins require metals to perform the biological function. ... ...

    Abstract The first-row D-block metal ions are essential for the physiology of living organisms, functioning as cofactors in metalloproteins or structural components for enzymes: almost half of all proteins require metals to perform the biological function. Understanding metal-protein interactions is crucial to unravel the mysteries behind molecular biology, understanding the effects of metal imbalance and toxicity or the diseases due to disorders in metal homeostasis. Metal-protein interactions are dynamic: they are noncovalent and affected by the environment to which the system is exposed. To reach a complete comprehension of the system, different conditions must be considered for the experimental investigation, in order to get information on the species distribution, the ligand coordination modes, complex stoichiometry and geometry. Thinking about the whole environment where a protein acts, investigations are often challenging, and simplifications are required to study in detail the mechanisms of metal interaction. This chapter is intended to help researchers addressing the problem of the complexity of metal-protein interactions, with particular emphasis on the use of peptides as model systems for the metal coordination site. The thermodynamic and spectroscopic methods most widely employed to investigate the interaction between metal ions and peptides in solution are here covered. These include solid-phase peptide synthesis, potentiometric titrations, calorimetry, electrospray ionization mass spectrometry, UV-Vis spectrophotometry, circular dichroism (CD), nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR). Additional experimental methods, which can be employed to study metal complexes with peptides, are also briefly mentioned. A case-study is finally reported providing a practical example of the investigation of metal-protein interaction by means of thermodynamic and spectroscopic methods applied to peptide model systems.
    Mesh-Begriff(e) Circular Dichroism ; Electron Spin Resonance Spectroscopy ; Spectrophotometry ; Thermodynamics ; Research Design ; Metals
    Chemische Substanzen Metals
    Sprache Englisch
    Erscheinungsdatum 2023-06-22
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1557-7988
    ISSN (online) 1557-7988
    DOI 10.1016/bs.mie.2023.05.004
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Investigation of metal interactions with YrpE protein of Bacillus subtilis by a polyhistidine peptide model.

    Bellotti, Denise / Leveraro, Silvia / Hecel, Aleksandra / Remelli, Maurizio

    Analytical biochemistry

    2023  Band 680, Seite(n) 115315

    Abstract: The use of model peptides that can simulate the behaviour of a protein domain is a very successful analytical method to study the metal coordination sites in biological systems. Here we study zinc and copper binding ability of the sequence HTHEHSHDHSHAH, ...

    Abstract The use of model peptides that can simulate the behaviour of a protein domain is a very successful analytical method to study the metal coordination sites in biological systems. Here we study zinc and copper binding ability of the sequence HTHEHSHDHSHAH, which serves as model for the metal interactions with YrpE, a putative metal-binding protein of the ZinT family identified in Bacillus subtilis. Compared to other ZinT proteins secreted by Gram-negative bacteria, the metal-coordination properties of YrpE N-terminal histidine-rich domain have not been yet characterized. Different independent analytical methods, aimed at providing information on the stability and structure of the formed species, have been employed, including potentiometric titrations, electrospray ionization mass spectrometry, UV-Vis spectrophotometry, circular dichroism and electron paramagnetic resonance spectroscopy. The obtained speciation models and equilibrium constants allowed to compare the metal-binding ability of the investigated polyhistidine sequence with that of other well-known histidine-rich peptides. Our thermodynamic results revealed that the YrpE domain HTHEHSHDHSHAH forms more stable metal complexes than other His-rich domains of similar ZinT proteins. Moreover, the studied peptide, containing the alternated (-XH-)
    Mesh-Begriff(e) Histidine ; Bacillus subtilis ; Peptides ; Metals ; Zinc
    Chemische Substanzen polyhistidine (26062-48-6) ; Histidine (4QD397987E) ; Peptides ; Metals ; Zinc (J41CSQ7QDS)
    Sprache Englisch
    Erscheinungsdatum 2023-09-07
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1110-1
    ISSN 1096-0309 ; 0003-2697
    ISSN (online) 1096-0309
    ISSN 0003-2697
    DOI 10.1016/j.ab.2023.115315
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: Impact of C- and N-terminal protection on the stability, metal chelation and antimicrobial properties of calcitermin.

    D'Accolti, Maria / Bellotti, Denise / Dzień, Emilia / Leonetti, Carlotta / Leveraro, Silvia / Albanese, Valentina / Marzola, Erika / Guerrini, Remo / Caselli, Elisabetta / Rowińska-Żyrek, Magdalena / Remelli, Maurizio

    Scientific reports

    2023  Band 13, Heft 1, Seite(n) 18228

    Abstract: The main limitation to the use of antimicrobial peptides (AMPs) as regular drugs, against antibiotic and antifungal resistance, mainly relates to their rapid degradation by proteolytic enzymes. The introduction of suitable structural changes in the ... ...

    Abstract The main limitation to the use of antimicrobial peptides (AMPs) as regular drugs, against antibiotic and antifungal resistance, mainly relates to their rapid degradation by proteolytic enzymes. The introduction of suitable structural changes in the peptide chain can make the peptide less susceptible to the action of proteases, thus overcoming this problem. To improve the plasma stability of calcitermin, a metal-chelating AMP present in the human respiratory tract and investigated in the present study, C- and/or N- terminal modifications have been introduced in the native sequence. Evaluation of peptide stability has been performed to determine the half-life times in human plasma of both native calcitermin and its derivatives. However, the protection of the peptide termini can also affect its metal coordination behaviour. Thus, the characterization of Zn
    Mesh-Begriff(e) Humans ; Anti-Bacterial Agents/chemistry ; Anti-Infective Agents ; Chelating Agents/pharmacology ; Chelating Agents/chemistry ; Circular Dichroism ; Copper/chemistry ; Mass Spectrometry ; Peptides/chemistry
    Chemische Substanzen Anti-Bacterial Agents ; Anti-Infective Agents ; Chelating Agents ; Copper (789U1901C5) ; Peptides ; calcitermin peptide, human
    Sprache Englisch
    Erscheinungsdatum 2023-10-25
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-023-45437-0
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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