scholarly journals Prevention of Oxidative DNA Degradation by Copper-Binding Peptides

2011 ◽  
Vol 75 (7) ◽  
pp. 1377-1379 ◽  
Author(s):  
Ken YOKAWA ◽  
Tomoko KAGENISHI ◽  
Tomonori KAWANO
Keyword(s):  
Dna Degradation ◽  
Copper Binding ◽  
Binding Peptides ◽  
Copper Binding Peptides

The Structural Study of Copper‐binding Peptides: Implication in the Aggregation of Amyloid‐β Peptides

2013 ◽  
Vol 60 (7) ◽  
pp. 891-897 ◽  
Author(s):  
Ren‐Jie Lin ◽  
Tzyy‐Rong Jinn ◽  
Soonmin Jang ◽  
Fur‐Der Mai ◽  
Feng‐Yin Li
Keyword(s):  
Structural Study ◽  
Amyloid Β ◽  
Copper Binding ◽  
Binding Peptides ◽  
Copper Binding Peptides

Copper‐Binding Peptides Attenuate Microglia Inflammation Through Suppression of NF‐kB Pathway

2021 ◽  
pp. 2100153
Author(s):  
Maria Elisa Caetano‐Silva ◽  
Laurie A. Rund ◽  
Mario Vailati‐Riboni ◽  
Maria Teresa Bertoldo Pacheco ◽  
Rodney W. Johnson
Keyword(s):  
Copper Binding ◽  
Binding Peptides ◽  
Copper Binding Peptides

Copper-Binding Peptides from Human Prion Protein and Newly Designed Peroxidative Biocatalysts

2011 ◽  
Vol 66 (3-4) ◽  
pp. 182-190
Author(s):  
Tomoko Kagenishi ◽  
Ken Yokawa ◽  
Takashi Kadono ◽  
Kazuya Uezu ◽  
Tomonori Kawano
Keyword(s):  
Prion Protein ◽  
Superoxide Anion ◽  
Active Catalyst ◽  
Copper Binding ◽  
Binding Motifs ◽  
Human Prion Protein ◽  
Binding Peptides ◽  
Superoxide Anion Radicals ◽  
Copper Binding Peptides ◽  
Catalytic Performances

A previous work suggested that peptides from the histidine-containing copper-binding motifs in human prion protein (PrP) function as peroxidase-like biocatalysts catalyzing the generation of superoxide anion radicals in the presence of neurotransmitters (aromatic monoamines) and phenolics such as tyrosine and tyrosyl residues on proteins. In this study, using various phenolic substrates, the phenol-dependent superoxide-generating activities of PrP-derived peptide sequences were compared. Among the peptides tested, the GGGTH pentapeptide was shown to be the most active catalyst for phenol-dependent reactions. Based on these results, we designed a series of oligoglycyl-histidines as novel peroxidative biocatalysts, and their catalytic performances including kinetics, heat tolerance, and freezing tolerance were analysed

scholarly journals A new approach to biomining: Bioengineering surfaces for metal recovery from aqueous solutions

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Jesica Urbina ◽  
Advait Patil ◽  
Kosuke Fujishima ◽  
Ivan G. Paulino-Lima ◽  
Chad Saltikov ◽  
...  
Keyword(s):  
Aqueous Solutions ◽  
Metal Binding ◽  
Raw Materials ◽  
Extraction Methods ◽  
Metal Recovery ◽  
Consumer Electronics ◽  
Metal Extraction ◽  
Copper Binding ◽  
Metal Binding Peptides ◽  
Binding Peptides

Abstract Electronics waste production has been fueled by economic growth and the demand for faster, more efficient consumer electronics. The glass and metals in end-of-life electronics components can be reused or recycled; however, conventional extraction methods rely on energy-intensive processes that are inefficient when applied to recycling e-waste that contains mixed materials and small amounts of metals. To make e-waste recycling economically viable and competitive with obtaining raw materials, recovery methods that lower the cost of metal reclamation and minimize environmental impact need to be developed. Microbial surface adsorption can aid in metal recovery with lower costs and energy requirements than traditional metal-extraction approaches. We introduce a novel method for metal recovery by utilizing metal-binding peptides to functionalize fungal mycelia and enhance metal recovery from aqueous solutions such as those found in bioremediation or biomining processes. Using copper-binding as a proof-of-concept, we compared binding parameters between natural motifs and those derived in silico, and found comparable binding affinity and specificity for Cu. We then combined metal-binding peptides with chitin-binding domains to functionalize a mycelium-based filter to enhance metal recovery from a Cu-rich solution. This finding suggests that engineered peptides could be used to functionalize biological surfaces to recover metals of economic interest and allow for metal recovery from metal-rich effluent with a low environmental footprint, at ambient temperatures, and under circumneutral pH.

Copper-chelating peptide from salmon by-product proteolysate

2020 ◽  
Vol 16 (4) ◽  
Author(s):  
Tam D.L. Vo ◽  
Khoa Trong Pham
Keyword(s):  
Amino Acid ◽  
G Protein ◽  
Binding Capacity ◽  
Protein A ◽  
Amino Acid Content ◽  
Copper Binding ◽  
Hydrolysis Time ◽  
Binding Peptides ◽  
Peptide Fractions ◽  
The Ideal

AbstractThe aims of this study included evaluation of copper-binding capacity (CBC) and amino acid composition of salmon by-product proteolysate and its peptide fractions, optimization of hydrolysis condition, and identification of copper-binding peptides from the proteolysate. The result was that under the ideal hydrolysis (Neutrase, temperature of 45 °C, pH 7, enzyme:substrate (E:S) proportion of 72.24 U/g protein and hydrolysis time of 8.02 h), the proteolysate had the indispensable amino acid content at approximately 38.7% and also displayed the maximal CBC of 15163.6 µg Cu2+/g protein. Besides, four peptide fractions of 10–30 kDa, 3–10 kDa, 1–3 kDa, and <1 kDa were recovered using ultrafiltration, among which the <1 kDa fraction had the highest CBC of 10852.00 ± 895.06 µgCu2+/g protein. A copper-binding peptide, Phe-Ile-Asp-Asp-Asp-Ala-Phe-Ile-Arg (1110 Da), was identified from this fraction using tandem mass spectrometry (MS/MS). As a whole, the proteolysate/peptides could be used for copper enhancement that could shield human body from copper inadequacy disorders.

Metallic prions

2004 ◽  
Vol 71 ◽  
pp. 193-202 ◽  
Author(s):  
David R Brown
Keyword(s):  
Prion Protein ◽  
Binding Capacity ◽  
Normal Function ◽  
Transmissible Spongiform Encephalopathies ◽  
Published Data ◽  
Normal Brain ◽  
Copper Binding ◽  
Loss Of Function ◽  
Spongiform Encephalopathies ◽  
The Brain

Prion diseases, also referred to as transmissible spongiform encephalopathies, are characterized by the deposition of an abnormal isoform of the prion protein in the brain. However, this aggregated, fibrillar, amyloid protein, termed PrPSc, is an altered conformer of a normal brain glycoprotein, PrPc. Understanding the nature of the normal cellular isoform of the prion protein is considered essential to understanding the conversion process that generates PrPSc. To this end much work has focused on elucidation of the normal function and activity of PrPc. Substantial evidence supports the notion that PrPc is a copper-binding protein. In conversion to the abnormal isoform, this Cu-binding activity is lost. Instead, there are some suggestions that the protein might bind other metals such as Mn or Zn. PrPc functions currently under investigation include the possibility that the protein is involved in signal transduction, cell adhesion, Cu transport and resistance to oxidative stress. Of these possibilities, only a role in Cu transport and its action as an antioxidant take into consideration PrPc's Cu-binding capacity. There are also more published data supporting these two functions. There is strong evidence that during the course of prion disease, there is a loss of function of the prion protein. This manifests as a change in metal balance in the brain and other organs and substantial oxidative damage throughout the brain. Thus prions and metals have become tightly linked in the quest to understand the nature of transmissible spongiform encephalopathies.

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