The structure of a copper complex of the growth factor glycyl-L-histidyl-L-lysine at 1.1 Å resolution

Perkins, Christopher; Rose, Norman J.; Weinstein, Boris; Stenkamp, Ronald E.; Jensen, L. H.; Pickart, Loren

doi:10.1016/s0020-1693(00)82544-x

Cited by 43 publications

(29 citation statements)

References 36 publications

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“…This affected the signals of γ, δ and ε protons of the Lys residue in Ni-HSA. The order of their shifts correlated well with ring-current calculations based on the geometry observed in the crystal structure of a copper complex with a short peptide containing both a histidine and a lysine residue, CuGHK, where the Lys side chain lies over the His ring [13].…”

Section: Albuminsupporting

confidence: 61%

“…The first one is located in the histone-fold domain (63 to 93 residues), and its model peptide was chosen as the 31-amino acid Ac-NSFVNDIFERIAG 13 [39].…”

Section: Histone H2bmentioning

confidence: 99%

“…At this pH, the labile amidic proton signals are lost and a well resolved solution structure of the Ni(II) complex was determined only for the 13 amino acid fragment, G 13 21 and Arg 24 on the lower one, could be relevant to the complex stability, limiting the access of water molecules to the binding site. Furthermore, the location of the Tyr 21 aromatic ring, close to the Ni(II) ion, can add extra stability to the complex via a possible interaction of the negative partial charge of the phenolic oxygen on the tyrosine with the positive part of the electrostatic potential generated by the nickel complex.…”

Section: Histone H2bmentioning

confidence: 99%

“…It has been shown [43,44] that Ni(II) underwent activation upon binding to HP2 [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15] peptide and became a DNA cleavage agent, so that this reactivity could be put in close relation with paternally transmitted transgenerational carcinogenesis in children of welders and machinists, professionally exposed to nickel-containing dusts and fumes [45].…”

Section: Protaminementioning

confidence: 99%

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The Involvement of Amino Acid Side Chains in Shielding the Nickel Coordination Site: An NMR Study

et al. 2013

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Abstract:Coordination of proteins and peptides to metal ions is known to affect their properties, often by a change in their structural organization. Side chains of the residues directly involved in metal binding or very close to the coordination centre may arrange themselves around it, in such a way that they can, for instance, disrupt the protein functions or stabilize a metal complex by shielding it from the attack of water or other small molecules. The conformation of these side chains may be crucial to different biological or toxic processes. In our research we have encountered such behaviour in several cases, leading to interesting results for our purposes. Here we give an overview on the structural changes involving peptide side chains induced by Ni(II) coordination. In this paper we deal with a number of peptides, deriving from proteins containing one or more metal coordinating sites, which have been studied through a series of NMR experiments in their structural changes caused by Ni(II) complexation. Several peptides have been included in the study: short sequences from serum albumin (HSA), Des-Angiotensinogen, the 30-amino acid tail of histone H4, some fragments from histone H2A and H2B, the initial fragment of human protamine HP2 and selected fragments from prion and Cap43 proteins. NMR was the election technique for gathering structural information. Experiments performed for this purpose included 1D 1 H and 13 C, and 2D HSQC, COSY, TOCSY, NOESY and ROESY acquisitions, which allowed the calculation of the Ni(II) complexes structural models.

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Section: Albuminsupporting

confidence: 61%

“…The first one is located in the histone-fold domain (63 to 93 residues), and its model peptide was chosen as the 31-amino acid Ac-NSFVNDIFERIAG 13 [39].…”

Section: Histone H2bmentioning

confidence: 99%

Section: Histone H2bmentioning

confidence: 99%

Section: Protaminementioning

confidence: 99%

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The Involvement of Amino Acid Side Chains in Shielding the Nickel Coordination Site: An NMR Study

et al. 2013

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“…Third, many peptide-based biomaterials are easily degraded by the body, thus making them desirable as drug delivery vehicles and tissue engineering scaffolds. Fourth, biology is replete with peptide sequences that exhibit structural transitions in response to the binding of metal ions and other biological ligands [13][14][15][16][17][18][19][20][21][22][23][24][25][26]; these sequences offer enormous possibilities in the design of biologically responsive materials.…”

Section: Introductionmentioning

confidence: 99%

Peptide-based biopolymers in biomedicine and biotechnology

Chow

Nunalee

Lim

et al. 2008

Materials Science and Engineering: R: Reports

286

231

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Peptides are emerging as a new class of biomaterials due to their unique chemical, physical, and biological properties. The development of peptide-based biomaterials is driven by the convergence of protein engineering and macromolecular self-assembly. This review covers the basic principles, applications, and prospects of peptide-based biomaterials. We focus on both chemically synthesized and genetically encoded peptides, including poly-amino acids, elastin-like polypeptides, silk-like polymers and other biopolymers based on repetitive peptide motifs. Applications of these engineered biomolecules in protein purification, controlled drug delivery, tissue engineering, and biosurface engineering are discussed.

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Metal Complexation with Langmuir Monolayers of Histidyl Peptide Lipids

et al. 2001

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Langmuir monolayers made from peptide-lipid molecules represent a novel direction in the research areas of biomimetic interfaces and two-dimensional supramolecular chemistry. Peptide structures and molecular recognition activities toward other guest molecules have been the focus of previous study. This study reports the investigation of metal complexation to histidine-containing peptide lipids in the organized Langmuir, Langmuir-Schaefer, or Langmuir-Blodgett films. Three peptide lipids PEP1-PEP3, with a histidine amino acid incorporated in the middle of the peptide, were designed and synthesized. The monolayer structures and metal-binding activities of each peptide lipid and their 1:1:1 molar ratio mixture were studied by thermodynamic and spectroscopic techniques. It was found that hard Lewis acid type metal cations such as K+ and Mg2+, and borderline or soft metal cations such as Zn2+, Cu2+, and Cd2+ exhibit clearly different binding activity toward peptide-lipid monolayers. The conformational changes of peptides upon binding with Cu2+ and Zn2+ were partially revealed by FT-IR spectroscopic studies. Furthermore, by adding a fluorescent-probe lipid to the peptide monolayer, dramatic fluorescence change was observed when Cu2+ or Zn2+ bound to the Langmuir and Langmuir-Schaefer films of peptide-lipid monolayers. Metal-protein complexation plays a crucial role in the function and activity of proteins and enzymes. Investigation of metal complexation to organized peptide Langmuir monolayers may provide an alternative approach for the development of artificial metalloproteins and novel supramolecular systems or materials.

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The structure of a copper complex of the growth factor glycyl-L-histidyl-L-lysine at 1.1 Å resolution

Cited by 43 publications

References 36 publications

The Involvement of Amino Acid Side Chains in Shielding the Nickel Coordination Site: An NMR Study

The Involvement of Amino Acid Side Chains in Shielding the Nickel Coordination Site: An NMR Study

Peptide-based biopolymers in biomedicine and biotechnology

Metal Complexation with Langmuir Monolayers of Histidyl Peptide Lipids

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