Coordination of Ni2+ and Cu2+ to metal ion binding domains of E. coli SlyD protein

Witkowska, Danuta; Valensin, Daniela; Rowińska‐Żyrek, Magdalena; Karafova, Anna; Kamysz, Wojciech; Kozłowski, Henryk

doi:10.1016/j.jinorgbio.2011.11.012

Cited by 24 publications

(18 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Such metal binding sites are obviously difficult to mimic by small peptides. However, a number of proteins possess relatively short histidine-rich sequences with strong metal binding ability, which substantially contributes to the function of the given macromolecule [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18]. Beside the well known human serum albumin (HSA) [1], probably the prion proteins (PrP) [2] are the most studied examples of such sequences.…”

Section: Introductionmentioning

confidence: 99%

“…Besides, several peptides copying the putative metal binding sequences of e.g. human α-synuclein [9], human endostatin [10], bacterial superoxide dismutases [11,12] and E. coli SlyD protein [13] have been studied to uncover fine functional details of the corresponding proteins. However, these metal binding sequences are part of less structured regions, frequently at the N-terminals, which may allow closer analogy in the metal binding properties of model peptides and native proteins.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

A minimalist chemical model of matrix metalloproteinases — Can small peptides mimic the more rigid metal binding sites of proteins?

Árus¹,

Nagy²,

Dancs³

et al. 2013

Journal of Inorganic Biochemistry

View full text Add to dashboard Cite

In order to develop a minimalist chemical model of matrix metalloproteinases (MMPs), we Around pH 6-7 the peptide, similarly to MMPs, offers {3N im } coordinated binding site for both zinc(II) and copper(II). In the case of copper(II), the formation of amide coordinated species at higher pH ceased the analogy with the copper(II) containing MMP variant. On the other hand, the zinc(II)-peptide system mimics some basic features of the MMP active sites: the main species around pH 7 (ZnH 2 L) possesses {3N im ,H 2 O} coordination environment, the deprotonation of the zinc-bound water takes place near to the physiological pH, it forms relatively stable ternary complexes with hydroxamic acids, and the species ZnH 2 L(OH) and ZnH 2 L(OH) 2 have notable hydrolytic activity between pH 7-9.

show abstract

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A minimalist chemical model of matrix metalloproteinases — Can small peptides mimic the more rigid metal binding sites of proteins?

Árus¹,

Nagy²,

Dancs³

et al. 2013

Journal of Inorganic Biochemistry

View full text Add to dashboard Cite

show abstract

“…Coordination of the amide nitrogen is confirmed by the absorption spectra, where a blue shift of the maximum (690 →620 nm) at pH 5-7 can be observed for the coordination of two nitrogens [17] (Figure 2A). The EPR spectrum at pH 6.5 (Figure S5A) shows overlapped signals for at least two Cu(II) species, most likely with 1N or 2N, or 2N or 3N coordination [18][19][20]. The distribution diagram, Figure S3A, supports the overlap of different complex species at this pH.…”

Section: Cu(ii) Complexesmentioning

confidence: 62%

Zn-Enhanced Asp-Rich Antimicrobial Peptides: N-Terminal Coordination by Zn(II) and Cu(II), Which Distinguishes Cu(II) Binding to Different Peptides

Miller

Matera-Witkiewicz

Mikołajczyk

et al. 2021

IJMS

Self Cite

View full text Add to dashboard Cite

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; however, as shown with potentiometry and absorption, CD and EPR spectroscopy, Asp residues in the first and/or second positions distinguish Cu(II) binding to SAAP3 and SAAP2 from their binding to SAAP6, decreasing the Cu(II) Lewis acidity and suppressing its square planar amide coordination by two pH units. We also show that these metal ions do not stabilize a membrane disrupting ability nor do they induce the antimicrobial activity of these peptides against a panel of human pathogens.

show abstract

“…It was shown that various ruthenium complexes are promising inhibitory agents, 265 and the similar effects of gold complexes was also demonstrated. 277 The latter ligand was able to bind only one metal ion at physiological pH while the formation of dinuclear complexes was also detected with the former peptide even in the presence of excess ligand. Human serum albumin is probably the best known and most studied histidine containing molecule with an outstanding Cu(II) and Ni(II) binding affinity.…”

Section: Metal Complexes Of Peptide Fragments Of Prion Proteinmentioning

confidence: 97%

Metal complexes of amino acids and peptides

Farkas¹,

Sóvágó²

2014

Amino Acids, Peptides and Proteins

View full text Add to dashboard Cite

show abstract

Coordination of Ni2+ and Cu2+ to metal ion binding domains of E. coli SlyD protein

Cited by 24 publications

References 41 publications

A minimalist chemical model of matrix metalloproteinases — Can small peptides mimic the more rigid metal binding sites of proteins?

A minimalist chemical model of matrix metalloproteinases — Can small peptides mimic the more rigid metal binding sites of proteins?

Zn-Enhanced Asp-Rich Antimicrobial Peptides: N-Terminal Coordination by Zn(II) and Cu(II), Which Distinguishes Cu(II) Binding to Different Peptides

Metal complexes of amino acids and peptides

Contact Info

Product

Resources

About