Identification of Binding Sites in Copper(II)-Peptide Complexes Using Infrared Spectroscopy DOI

Zhenghangcheng Li,

Feng Xue-yu,

Kaijun Yuan

et al.

The Journal of Physical Chemistry B, Journal Year: 2024, Volume and Issue: 128(8), P. 1884 - 1891

Published: Feb. 20, 2024

Complex formation of the copper(II) ion (CuII) with histidine (H) and H-containing peptides plays a crucial role in various metallo-enzymatic reactions. To elucidate nature coordinate bonding CuII complexes, Fourier-transform infrared spectroscopy 2D IR were employed to investigate coordination geometries diglycine, l-histidylglycine (HG), glycyl-l-histidine (GH), glycylglycyl-l-histidine. The different peptide groups, including N- C-termini, amide group, imidazole H side chain, exhibits distinct spectral features. derived molecular structure CuII–HG complex based on these features significantly differs from that CuII–GH, suggesting preference N-terminus steric hindrance chain chelation.

Language: Английский

Antimicrobial Peptides and Copper(II) Ions: Novel Therapeutic Opportunities DOI

Jasmin Portelinha,

Searle S. Duay,

Seung I. Yu

et al.

Chemical Reviews, Journal Year: 2021, Volume and Issue: 121(4), P. 2648 - 2712

Published: Feb. 1, 2021

The emergence of new pathogens and multidrug resistant bacteria is an important public health issue that requires the development novel classes antibiotics. Antimicrobial peptides (AMPs) are a promising platform with great potential for identification lead compounds can combat aforementioned due to their broad-spectrum antimicrobial activity relatively low rate resistance emergence. AMPs multicellular organisms made debut four decades ago thanks ingenious researchers who asked simple questions about bacterial infections insects. Questions such as "Do fruit flies ever get sick?", combined pioneering studies, have led understanding universal weapons immune system. This review focuses on subclass feature metal binding motif known amino terminal copper nickel (ATCUN) motif. One metal-based strategies hosts facing pathogen, it includes wielding inherent toxicity deliberately trafficking this ion into sites infection. sudden increase in concentration ions presence ATCUN-containing (ATCUN-AMPs) likely results synergistic interaction. Herein, we examine common structural features ATCUN-AMPs exist across species, highlight unique deserve additional attention. We also present current state knowledge molecular mechanisms behind methods available study class AMPs.

Language: Английский

Citations

83
Extracellular Cu2+ pools and their detection: From current knowledge to next-generation probes DOI Creative Commons
Enrico Falcone, Michael Okafor, Nicolas Vitale

et al.

Coordination Chemistry Reviews, Journal Year: 2021, Volume and Issue: 433, P. 213727 - 213727

Published: Feb. 8, 2021

Language: Английский

Citations

73
Montmorillonite-supported Cu-tripeptide complex for efficient Congo red degradation DOI

Mounir Mekidiche,

Khadidja Khaldi,

Djahida Lerari‐Zinai

et al.

Materials Chemistry and Physics, Journal Year: 2025, Volume and Issue: 339, P. 130640 - 130640

Published: March 17, 2025

Citations

1
Designed Metal-ATCUN Derivatives: Redox- and Non-redox-Based Applications Relevant for Chemistry, Biology, and Medicine DOI Creative Commons
Biplab K. Maiti,

Nidhi Govil,

Taraknath Kundu

et al.

iScience, Journal Year: 2020, Volume and Issue: 23(12), P. 101792 - 101792

Published: Nov. 10, 2020

The designed "ATCUN" motif (amino-terminal copper and nickel binding site) is a replica of naturally occurring ATCUN site found in many proteins/peptides, an attractive platform for multiple applications, which include nucleases, proteases, spectroscopic probes, imaging, small molecule activation. motifs are engineered at periphery by conjugation to recombinant proteins, peptides, fluorophores, or recognition domains through chemically genetically, fulfilling the needs various biological relevance wide range practical usages. This chemistry has witnessed significant growth over last few decades several interesting derivatives have been described. redox role moieties also important aspect be considered. potential M-ATCUN modulated judicious choice amino acid (including stereochemistry, charge, position) that ultimately leads catalytic efficiency. In this context, purposefully redox- non-redox-based including target-based metallodrugs, inhibition amyloid-β toxicity, telomere shortening, enzyme inactivation, biomolecules stitching modification, next-generation antibiotic,

Language: Английский

Citations

43
Key Intermediate Species Reveal the Copper(II)‐Exchange Pathway in Biorelevant ATCUN/NTS Complexes DOI Creative Commons
Radosław Kotuniak, Marc J. F. Strampraad, Karolina Bossak‐Ahmad

et al.

Angewandte Chemie International Edition, Journal Year: 2020, Volume and Issue: 59(28), P. 11234 - 11239

Published: April 8, 2020

Abstract The amino‐terminal copper and nickel/N‐terminal site (ATCUN/NTS) present in proteins bioactive peptides exhibits high affinity towards Cu II ions have been implicated human physiology. Little is known, however, about the rate exact mechanism of formation such complexes. We used stopped‐flow microsecond freeze‐hyperquenching (MHQ) techniques supported by steady‐state spectroscopic electrochemical data to demonstrate partially coordinated intermediate complexes formed glycyl–glycyl–histidine (GGH) peptide, simplest ATCUN/NTS model. One these novel intermediates, characterized two‐nitrogen coordination, t 1/2 ≈100 ms at pH 6.0 ability maintain /Cu I redox pair best candidate for long‐sought reactive species extracellular transport.

Language: Английский

Citations

40
Modulation of 3D Bioprintability in Polysaccharide Bioink by Bioglass Nanoparticles and Multiple Metal Ions for Tissue Engineering DOI
Amitava Bhattacharyya,

Mst Rita Khatun,

S. Narmatha

et al.

Tissue Engineering and Regenerative Medicine, Journal Year: 2023, Volume and Issue: 21(2), P. 261 - 275

Published: Nov. 18, 2023

Language: Английский

Citations

15
Bioinorganic chemistry of shepherin II complexes helps to fight Candida albicans? DOI

Klaudia Szarszoń,

Aleksandra Mikołajczyk,

Manuela Grelich-Mucha

et al.

Journal of Inorganic Biochemistry, Journal Year: 2024, Volume and Issue: 253, P. 112476 - 112476

Published: Jan. 3, 2024

Language: Английский

Citations

5
How trimerization of CTR1 N-terminal model peptides tunes Cu-binding and redox-chemistry DOI Creative Commons

Thibaut Galler,

Vincent Lebrun, Laurent Raibaut

et al.

Chemical Communications, Journal Year: 2020, Volume and Issue: 56(81), P. 12194 - 12197

Published: Jan. 1, 2020

Trimeric arrangement of model peptides the CTR1 N-terminus promotes Cu(ii) reduction and Cu(i) binding.

Language: Английский

Citations

33
Impact of N‐Truncated Aβ Peptides on Cu‐ and Cu(Aβ)‐Generated ROS: CuI Matters! DOI
Charlène Esmieu, Guillaume Ferrand, Valentina Borghesani

et al.

Chemistry - A European Journal, Journal Year: 2020, Volume and Issue: 27(5), P. 1777 - 1786

Published: Oct. 15, 2020

Abstract In vitro Cu(Aβ 1– x )‐induced ROS production has been extensively studied. Conversely, the ability of N ‐truncated isoforms Aβ to alter Cu‐induced overlooked, even though they are main constituents amyloid plaques found in human brain. ‐Truncated peptides at positions 4 and 11 (Aβ 4– 11– ) contain an amino‐terminal copper nickel (ATCUN) binding motif (H 2 N‐Xxx‐Zzz‐His) that confer them different coordination sites higher affinities for Cu II compared peptide. It further proposed role peptide is quench toxicity However, I not investigated date. contrast , expected be same ‐intact peptides. Herein, we report in‐depth characterizations studies (Cu complexes 4–16 11–16 Our findings show do produce when present medium, albeit a lesser extent than unmodified counterpart. addition, used as competitor ligands (i.e., presence 1–16 ), able fully preclude production.

Language: Английский

Citations

31
Modulating Copper(II) Coordination and Antimicrobial Activity: Effects of d-Amino Acid Substitution and Retro-Inverso Modification in Human Saliva MUC7 Peptide DOI Creative Commons
Joanna Wątły,

Klaudia Szarszoń,

Monika Sabieraj

et al.

Inorganic Chemistry, Journal Year: 2025, Volume and Issue: unknown

Published: March 19, 2025

Fragments of MUC7, a salivary protein involved in nonimmune defense, arise from proteolytic cleavage saliva and exhibit antimicrobial properties. However, their therapeutic use is limited by low stability due to further degradation. To address this, native MUC7 fragment was modified using d-amino acids the retro-inverso strategy. Given role metal ions enhancing peptides, we analyzed bioinorganic chemistry these systems with Cu(II) assessed activity against fungal bacterial strains. This study first explore correlation between binding mode, structure, stability, peptides as well coordination such systems. A combination experimental techniques (potentiometry, mass spectrometry, UV–vis, circular dichroism, electron paramagnetic resonance, nuclear magnetic resonance spectroscopy) density functional theory calculations characterized chemistry. Our results demonstrate that "standard" enantiomeric exchange modifications have minimal effect on secondary structure biological studied complexes. significantly influence thermodynamic

Language: Английский

Citations

0