ArticleInternational journal of molecular sciences2016
Coordination Environment of Cu(II) Ions Bound to N-Terminal Peptide Fragments of Angiogenin Protein.
Article in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 35 citations in OpenAlex.
- The Two Faces of Copper Capture Driven by the Internal His/Met-Rich and N-Terminal His-Rich Domains of CopI.Inorganic chemistry · 2026Article
- Alverine-Loaded Lipid Bilayer-Graphene Oxide Hybrids as a Novel Nanomedicine Platform for Neural Cancer.International journal of molecular sciences · 2026Article
- Thiol, His-His Motif, and the Battle over Cu(II) in the Relationship of CopM Metallophore and OprC Outer Membrane Protein.Inorganic chemistry · 2025Article
- The Hybrid Nano-Biointerface between Proteins/Peptides and Two-Dimensional Nanomaterials.Molecules (Basel, Switzerland) · 2023Review
- Bioinspired Nanoplatforms Based on Graphene Oxide and Neurotrophin-Mimicking Peptides.Membranes · 2023Article
- Angiogenesis in Disease.International journal of molecular sciences · 2022Article
- Angiogenin and Copper Crossing in Wound Healing.International journal of molecular sciences · 2021Review
- Peptides Derived from Angiogenin Regulate Cellular Copper Uptake.International journal of molecular sciences · 2021Article
- Nerve Growth Factor Peptides Bind Copper(II) with High Affinity: A Thermodynamic Approach to Unveil Overlooked Neurotrophin Roles.International journal of molecular sciences · 2021Article
- Gold Nanoparticles Functionalized with Angiogenin for Wound Care Application.Nanomaterials (Basel, Switzerland) · 2021Article
- The Ionophoric Activity of a Pro-Apoptotic VEGF165 Fragment on HUVEC Cells.International journal of molecular sciences · 2020Article
- Exploring the Specificity of Rationally Designed Peptides Reconstituted from the Cell-Free Extract ofInorganic chemistry · 2020Article
- A Tunable Nanoplatform of Nanogold Functionalised with Angiogenin Peptides for Anti-Angiogenic Therapy of Brain Tumours.Cancers · 2019Article
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Authors and funding
9 authors at 5 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Angiogenin (Ang) is a potent angiogenic factor, strongly overexpressed in patients affected by different types of cancers. The specific Ang cellular receptors have not been identified, but it is known that Ang-actin interaction induces changes both in the cell cytoskeleton and in the extracellular matrix. Most in vitro studies use the recombinant form (r-Ang) instead of the form that is normally present in vivo ("wild-type", wt-Ang). The first residue of r-Ang is a methionine, with a free amino group, whereas wt-Ang has a glutamic acid, whose amino group spontaneously cyclizes in the pyro-glutamate form. The Ang biological activity is influenced by copper ions. To elucidate the role of such a free amino group on the protein-copper binding, we scrutinized the copper(II) complexes with the peptide fragments Ang(1-17) and AcAng(1-17), which encompass the sequence 1-17 of angiogenin (QDNSRYTHFLTQHYDAK-NH₂), with free amino and acetylated N-terminus, respectively. Potentiometric, ultraviolet-visible (UV-vis), nuclear magnetic resonance (NMR) and circular dichroism (CD) studies demonstrate that the two peptides show a different metal coordination environment. Confocal microscopy imaging of neuroblastoma cells with the actin staining supports the spectroscopic results, with the finding of different responses in the cytoskeleton organization upon the interaction, in the presence or not of copper ions, with the free amino and the acetylated N-terminus peptides.
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