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Zinc(ii) binding ability of tri-, tetra- and penta-peptides containing two or three histidyl residues

https://doi.org/10.1039/b706303b
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/1099-0682(200203)2002:3<761::aid-ejic761>3.0.co;2-vopenalex-snapshot
Dipeptides Made up Solely from Histidine: Solution Behaviour and Zinc Complexation
inferredcites →https://doi.org/10.1002/cber.19951280603openalex-snapshot
Zinc Complexes of Histidine‐Containing Di‐ and Tripeptides
inferredcites →https://doi.org/10.1002/cber.19961291016openalex-snapshot
Zinc Complexes of Amino Acids and Peptides, 8[]. Difunctional Dipeptides Containing Cysteine or Histidine: Solution Behavior and Zinc Complextion
inferredcites →https://doi.org/10.1002/chin.198306081openalex-snapshot
ChemInform Abstract: STUDIES ON TRANSITION METAL‐PEPTIDE COMPLEXES. PART 7. COPPER(II) COMPLEXES OF DIPEPTIDES CONTAINING L‐HISTIDINE
inferredcites →https://doi.org/10.1016/0039-9140(96)01958-3openalex-snapshot
Investigation of equilibria in solution. Determination of equilibrium constants with the HYPERQUAD suite of programs
inferredcites →https://doi.org/10.1016/j.jinorgbio.2003.09.012openalex-snapshot
Copper(II) and zinc(II) complexes of the peptides Ac-HisValHis-NH 2 and Ac-HisValGlyAsp-NH 2 related to the active site of the enzyme CuZnSOD
inferredcites →https://doi.org/10.1016/j.jinorgbio.2006.04.003openalex-snapshot
Transition metal complexes of terminally protected peptides containing histidyl residues
inferredcites →https://doi.org/10.1016/s0003-2670(01)80616-4openalex-snapshot
A study of some problems in determining the stoicheiometric proton dissociation constants of complexes by potentiometric titrations using a glass electrode
inferredcites →https://doi.org/10.1016/s0010-8545(98)00261-6openalex-snapshot
Specific structure–stability relations in metallopeptides
inferredcites →https://doi.org/10.1016/s0020-1693(01)00561-8openalex-snapshot
Zinc complexation of cyclic dipeptides containing cysteine and/or histidine
inferredcites →https://doi.org/10.1016/s0020-1693(97)05875-1openalex-snapshot
Solution behaviour and zinc complexation of tripeptides with cysteine and/or histidine at both termini
inferredcites →https://doi.org/10.1016/s0020-1693(98)00230-8openalex-snapshot
Potentiometric and spectroscopic studies of transition metal complexes of bis(imidazolyl) and bis(pyridyl) derivatives of amino acids
inferredcites →https://doi.org/10.1016/s0162-0134(01)00204-5openalex-snapshot
Interaction of Cu2+ with His–Val–His and of Zn2+ with His–Val–Gly–Asp, two peptides surrounding metal ions in Cu,Zn-superoxide dismutase enzyme
inferredcites →https://doi.org/10.1016/s1387-3806(03)00221-5openalex-snapshot
Zinc binding properties of the amyloid fragment Aβ(1–16) studied by electrospray-ionization mass spectrometry
inferredcites →https://doi.org/10.1021/ac960117zopenalex-snapshot
Multicomponent NMR Titration for Simultaneous Measurement of Relative pKas
inferredcites →https://doi.org/10.1021/cr00050a003openalex-snapshot
Coordinating properties of the amide bond. Stability and structure of metal ion complexes of peptides and related ligands
inferredcites →https://doi.org/10.1021/cr950042jopenalex-snapshot
Recent Advances in Zinc Enzymology
inferredcites →https://doi.org/10.1021/ja00309a001openalex-snapshot
Nuclear magnetic resonance studies of the solution chemistry of metal complexes. 21. The complexation of zinc by glycylhistidine and alanylhistidine peptides
inferredcites →https://doi.org/10.1021/jp047515nopenalex-snapshot
New Protonation Microequilibrium Treatment in the Case of Some Amino Acid and Peptide Derivatives Containing a Bis(imidazolyl)methyl Group
inferredcites →https://doi.org/10.1039/b407909dopenalex-snapshot
Copper( ii ) complexes of N-terminal protected tri- and tetra-peptides containing histidine residues
inferredcites →https://doi.org/10.1039/b607515kopenalex-snapshot
Metal ion selectivity of oligopeptides
inferredcites →https://doi.org/10.1039/b608190hopenalex-snapshot
Copper( ii ) complexes of terminally protected pentapeptides containing three histidyl residues in alternating positions, Ac-His-Xaa-His-Yaa-His-NH 2
inferredcites →https://doi.org/10.1039/dt9820002159openalex-snapshot
Studies on transition-metal–peptide complexes. Part 7. Copper( II ) complexes of dipeptides containing L -histidine
inferredcites →https://doi.org/10.1039/dt9850001195openalex-snapshot
SUPERQUAD: an improved general program for computation of formation constants from potentiometric data
inferredcites →https://doi.org/10.1074/jbc.m100175200openalex-snapshot
Alzheimer's Disease Amyloid-β Binds Copper and Zinc to Generate an Allosterically Ordered Membrane-penetrating Structure Containing Superoxide Dismutase-like Subunits
inferredcites →https://doi.org/10.1074/jbc.m504454200openalex-snapshot
Structural Changes of Region 1-16 of the Alzheimer Disease Amyloid β-Peptide upon Zinc Binding and in Vitro Aging
inferredcites →https://doi.org/10.1155/s1565363303000086openalex-snapshot
Interaction of Cu(II)with His‐Val‐Gly‐Asp and of Zn(II)with His‐Val‐His, Two Peptides at the Active Site ofCu,Zn‐Superoxide Dismutase
inferredcites →https://doi.org/10.1248/cpb.45.1108openalex-snapshot
Proton Nuclear Magnetic Resonance Studies of the Complexation of Zn(II) with Histidine-Containing Peptides, L-histidyl-L-histidylglycylglycine and L-histidylglycyl-L-histidylglycine.
inferredcites →https://doi.org/10.1248/jhs.52.1openalex-snapshot
Zinc Neurotoxicity and its Role in Neurodegenerative Diseases

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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In Vitro Digestion Analysis of Soft Candy Containing Peptide-Zinc Chelate Derived from Low-Fluoride Protein Hydrolysates of Antarctic Krill (Euphausia Superba)
inferred← citeshttps://doi.org/10.1002/chem.201101364openalex-snapshot
Zinc(II) Complexes of Ubiquitin: Speciation, Affinity and Binding Features
inferred← citeshttps://doi.org/10.1002/chem.201203545openalex-snapshot
Harnessing the Flexibility of Peptidic Scaffolds to Control their Copper(II)‐Coordination Properties: A Potentiometric and Spectroscopic Study
inferred← citeshttps://doi.org/10.1016/bs.mie.2017.07.012openalex-snapshot
pH-Free Measurement of Relative Acidities, Including Isotope Effects
inferred← citeshttps://doi.org/10.1016/j.ccr.2016.04.015openalex-snapshot
Coordinating properties of peptides containing histidyl residues
inferred← citeshttps://doi.org/10.1016/j.fbio.2024.104188openalex-snapshot
Production of novel mung bean peptides-based zinc supplement: Process optimization, chelation mechanism, and stability assessment in vitro
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Particulate nanocomposite from oyster ( Crassostrea rivularis ) hydrolysates via zinc chelation improves zinc solubility and peptide activity
inferred← citeshttps://doi.org/10.1016/j.foodchem.2020.128056openalex-snapshot
Preparation process optimization, structural characterization and in vitro digestion stability analysis of Antarctic krill (Euphausia superba) peptides-zinc chelate
inferred← citeshttps://doi.org/10.1016/j.foodchem.2026.150711openalex-snapshot
Production of a novel black soldier fly larvae (Hermetia illucens) protein hydrolysate-zinc chelate: Characterization, chelation mechanism, and zinc solubility
inferred← citeshttps://doi.org/10.1016/j.fufo.2024.100390openalex-snapshot
In vitro digestion analysis of soft candy containing peptide-zinc chelates derived from low-fluoride protein hydrolysates of Antarctic krill (Euphausia superba) powder
inferred← citeshttps://doi.org/10.1016/j.ica.2008.01.022openalex-snapshot
Thermodynamic and structural characterization of the macrochelates formed in the reactions of copper(II) and zinc(II) ions with peptides of histidine
inferred← citeshttps://doi.org/10.1016/j.ica.2008.04.001openalex-snapshot
Metal-binding ability of histidine-containing peptidehydroxamic acids: Imidazole versus hydroxamate coordination
inferred← citeshttps://doi.org/10.1016/j.ica.2014.11.012openalex-snapshot
Copper(II), nickel(II) and zinc(II) complexes of hexapeptides containing separate aspartyl and histidyl residues
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2008.04.007openalex-snapshot
Copper and zinc binding properties of the N-terminal histidine-rich sequence of Haemophilus ducreyi Cu,Zn superoxide dismutase
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2009.09.002openalex-snapshot
Probing the Cu2+ and Zn2+ binding affinity of histidine-rich glycoprotein
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2010.04.008openalex-snapshot
Nickel(II) complexes of the multihistidine peptide fragments of human prion protein
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2012.02.014openalex-snapshot
Mixed metal copper(II)-nickel(II) and copper(II)-zinc(II) complexes of multihistidine peptide fragments of human prion protein
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2013.07.008openalex-snapshot
Binary and ternary mixed metal complexes of terminally free peptides containing two different histidyl binding sites
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2013.09.021openalex-snapshot
The copper(II) and zinc(II) coordination mode of HExxH and HxxEH motif in small peptides: The role of carboxylate location and hydrogen bonding network
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2015.06.020openalex-snapshot
Copper(II) and nickel(II) binding sites of peptide containing adjacent histidyl residues
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2016.08.013openalex-snapshot
Influence of the N-terminus acetylation of Semax, a synthetic analog of ACTH(4-10), on copper(II) and zinc(II) coordination and biological properties
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2026.113429openalex-snapshot
Peptide and peptide-protein models of the plastocyanin copper-binding site
inferred← citeshttps://doi.org/10.1016/j.pep.2013.03.015openalex-snapshot
Cloning, purification and metal binding of the HNH motif from colicin E7
inferred← citeshttps://doi.org/10.1016/j.poly.2013.06.014openalex-snapshot
The effect of non-coordinating side chains on the metal binding affinities of peptides of histidine
inferred← citeshttps://doi.org/10.1021/acs.inorgchem.5c00672openalex-snapshot
Metal-Induced Amide Deprotonation and Binding Typical for Cu(II), Not Possible for Zn(II) and Fe(II)
inferred← citeshttps://doi.org/10.1021/ic401318topenalex-snapshot
Zinc(II) Interactions with Brain-Derived Neurotrophic Factor N-Terminal Peptide Fragments: Inorganic Features and Biological Perspectives
inferred← citeshttps://doi.org/10.1021/ic802190vopenalex-snapshot
Interaction of Copper(II) with the Prion Peptide Fragment HuPrP(76−114) Encompassing Four Histidyl Residues within and outside the Octarepeat Domain
inferred← citeshttps://doi.org/10.1021/ic9008202openalex-snapshot
Heteronuclear and Homonuclear Cu2+ and Zn2+ Complexes with Multihistidine Peptides Based on Zebrafish Prion-like Protein
inferred← citeshttps://doi.org/10.1021/ic9012334openalex-snapshot
Metal Loading Capacity of Aβ N-Terminus: a Combined Potentiometric and Spectroscopic Study of Zinc(II) Complexes with Aβ(1−16), Its Short or Mutated Peptide Fragments and Its Polyethylene Glycol−ylated Analogue
inferred← citeshttps://doi.org/10.1021/jp411655eopenalex-snapshot
Environmental Influence on Zn–Histidine Complexes under No-Packing Conditions
inferred← citeshttps://doi.org/10.1039/b808323aopenalex-snapshot
Complex formation processes of terminally protected peptides containing two or three histidyl residues. Characterization of the mixed metal complexes of peptides
inferred← citeshttps://doi.org/10.1039/b811224jopenalex-snapshot
Zn(ii) ions bind very efficiently to tandem repeat region of “prion related protein” (PrP-rel-2) of zebra-fish. MS and potentiometric evidence
inferred← citeshttps://doi.org/10.1039/b811452hopenalex-snapshot
Approaching the minimal metal ion binding peptide for structural and functional metalloenzyme mimicking
inferred← citeshttps://doi.org/10.1039/b816498copenalex-snapshot
Transition metal complexes of short multihistidine peptides
inferred← citeshttps://doi.org/10.1039/b903721gopenalex-snapshot
Copper(ii) and zinc(ii) ion binding properties of a MAP type branched ligand with histidines as surface functionalities
inferred← citeshttps://doi.org/10.1039/b905871kopenalex-snapshot
Metal complexes of amino acids and amino acid side chain groups. Structures and properties
inferred← citeshttps://doi.org/10.1039/c4dt00903gopenalex-snapshot
The specificity of interaction of Zn 2+ , Ni 2+ and Cu 2+ ions with the histidine-rich domain of the TjZNT1 ZIP family transporter
inferred← citeshttps://doi.org/10.1039/c5dt00945fopenalex-snapshot
Zn II and Hg II binding to a designed peptide that accommodates different coordination geometries
inferred← citeshttps://doi.org/10.1039/c6nj00081aopenalex-snapshot
Nickel( ii ), zinc( ii ) and cadmium( ii ) complexes of hexapeptides containing separate histidyl and cysteinyl binding sites
inferred← citeshttps://doi.org/10.1039/c7dt00456gopenalex-snapshot
Metal coordination of ferrocene–histidine conjugates
inferred← citeshttps://doi.org/10.1039/c8nj04538kopenalex-snapshot
Metal binding selectivity of an N-terminally free multihistidine peptide HAVAHHH-NH 2
inferred← citeshttps://doi.org/10.1039/c9mt00131jopenalex-snapshot
Stability of Cu( ii ) complexes with FomA protein fragments containing two His residues in the peptide chain
inferred← citeshttps://doi.org/10.1039/d5dt03057aopenalex-snapshot
How do copper( ii ) and zinc( ii ) bind to tau protein, and how might this promote aggregation?
inferred← citeshttps://doi.org/10.1155/2007/30394openalex-snapshot
Thermodynamic and Structural Characterization of the Copper(II) Complexes of Peptides Containing Both Histidyl and Aspartyl Residues
inferred← citeshttps://doi.org/10.14232/phd.1863openalex-snapshot
A colicin E7 nukleáz domén, mint egy lehetséges mesterséges metallonukleáz alapja
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Preparation, Characterization, and In Vitro Stability Analysis of Deer Sinew Peptide-Zinc Chelate
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inferred← citeshttps://doi.org/10.3390/molecules27113435openalex-snapshot
The Role of Side Chains in the Fine-Tuning of the Metal-Binding Ability of Multihistidine Peptides
inferred← citeshttps://doi.org/10.3390/pharmaceutics15030935openalex-snapshot
Designing Formulation Strategies for Enhanced Stability of Therapeutic Peptides in Aqueous Solutions: A Review
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