A novel copper (II) binding peptide for a colorimetric biosensor system design

Korkmaz, Nuriye; Hwang, Changhyun; Kessler, Kim Kristin; Silina, Yuliya E.; Müller, Lisann; Park, Jayoung

doi:10.1016/j.talanta.2021.122439

Cited by 13 publications

(16 citation statements)

References 33 publications

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“…Our previously identified Cu(II) binding peptide candidates were as well rich in N-containing functional groups implying their role in metal ion binding process. [18] Moreover, the presence of carbonyl oxygen groups could contribute the peptide-metal ion complexation as such that a peptide can bind metal ions through an amide nitrogen or a carbonyl oxygen group. [28,29] Interestingly, all four candidate Pb(II) specific peptides reported in this study had carbonyl oxygen groups which might have played a role in Pb(II) binding process.…”

Section: Resultsmentioning

confidence: 99%

“…Until now, plenty of peptides have been reported which were identified through phage display screening technique. Some examples include metal ion binding peptides specific for Cu(II) [ 18 ] , Ni(II) [ 19 ] , Cr(III) [ 20 ] , cancer cell targeting peptides [ 21 ] , enzyme inhibitors [ 22 ] , antibody fragments, [ 23 ] and material binding peptides [ 24 ] .…”

Section: Introductionmentioning

confidence: 99%

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Phage display selection of a Pb(II) specific peptide and its application as a biorecognition unit for colorimetric detection of Pb(II) ions

Korkmaz,

Kim

2023

Biotechnology Journal

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Phage display technology employs a library of engineered filamentous M13 viruses infecting only bacteria. In this study, the genuine phage display selection technique was applied to identify a Pb(II) specific peptide. After three rounds of positive selection against Pb(II) coated agarose‐based beads and the consecutive negative screenings against interfering metal ions (Al(III), Co(II), Fe(III), Ni(II), and Zn(II)), a final phage library with enhanced Pb(II) binding was obtained. Enzyme Linked Immunosorbent Assay (ELISA) analyses confirmed the selective Pb(II) binding of the enriched viruses. Twenty monoclonal phage plaques were randomly selected, single stranded DNAs (ssDNAs) were isolated and sequenced. Sequencing results revealed four different peptide sequences. Pb9 peptide (KASPYIT) showing the most specific Pb(II) binding was selected for detection studies. Pb9 was synthetically synthesized with additional three cysteine (3xCys) units at C‐terminal. Twenty nanometers AuNPs were functionalized with Pb9‐3xCys peptides through Au‐thiol (Au‐S) interaction. A colorimetric Pb(II) detection system was validated using the engineered peptide‐AuNP complex at a calculated LOD of around 11 nM (3σ/k, n = 6) for the case study. The detection system was Pb(II) selective over various metal ions (Ag(II), Al(III), Au(III), Cd(II), Co(II), Cr (III), Cu(II), Fe(III), Hg(II), Mg(II), Mn(II), Ni(II), and Zn(II)). Such metal ion specific peptides can be further studied to develop simple, user friendly and cost‐effective tools to design alternative detection and bioremediation systems for a circular economy.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Phage display selection of a Pb(II) specific peptide and its application as a biorecognition unit for colorimetric detection of Pb(II) ions

Korkmaz,

Kim

2023

Biotechnology Journal

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“…In this study, we investigated the stability of the adsorption layer of the CBP–RGD and the scaffolding function. Solid binding peptides have recently been used in anti‐infection drugs (Beddingfield et al, 2021), tissue repair (Shortt et al, 2020; Tolg et al, 2012), and heavy metal ion detection systems (Korkmaz et al, 2021). A notable advantage of the solid binding peptide is one‐pot biofunctionalization (Migita et al, 2020; Sakaguchi‐Mikami et al, 2020).…”

Section: Discussionmentioning

confidence: 99%

Binding stability of peptides to Co–Cr–Mo alloy affects proliferation and differentiation of osteoblast

Migita

Wakabayashi

Yamazaki

2022

Biotech & Bioengineering

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Cobalt–chromium–molybdenum (CCM) alloys possess high corrosion‐resistant properties as well as good mechanical properties. Hence, the alloys are employed in medical implants such as artificial knee and hip joints, coronary stents, and removable partial dentures. To improve the biocompatibility of CCM alloys, we reported that CCM‐binding peptide (CBP) linked to cell‐adhesive motif Arg–Gly–Asp (RGD) improved the attachment of endothelial cells on CCM alloys. However, the stability of CBP adsorption on the alloy and its effect on osteoblast compatibility are still unclear. In this study, we evaluated the stabilization of the adsorption layer of CBP–RGD on CCM alloy surface and investigated the effect of CBP–RGD peptide on the proliferation and differentiation of the osteoblasts. CBP–RGD layer exhibited higher stabilization than the RGD adsorption layer for 7 days. In addition, the proliferation of osteoblast on CBP–RGD adsorbed alloy higher than that on RGD adsorbed alloy. Moreover, the calcification of cells cultured on the CBP–RGD adsorbed alloy was significantly higher than that of the cells on RGD adsorbed alloy. These findings indicate that the CBP binding was stable during the culture of osteoblasts on the CCM alloy.

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“…Peptides and proteins can be rapidly adsorbed or assembled on the surface of AuNPs to trigger or prevent the aggregation of AuNPs. Based on the coordination of Cu 2+ with peptide, AuNPs-based colorimetric methods have been used for the quantification of peptide and Cu 2+ ( Table 2 ) [ 58 , 59 , 60 , 61 ]. For example, Wang et al investigated the interaction between amyloid-β peptides and Cu 2+ /Zn 2+ ions using AuNPs as the indicators [ 59 ].…”

Section: Colorimetric Biosensorsmentioning

confidence: 99%

Progress in the Development of Biosensors Based on Peptide–Copper Coordination Interaction

et al. 2022

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Copper ions, as the active centers of natural enzymes, play an important role in many physiological processes. Copper ion-based catalysts which mimic the activity of enzymes have been widely used in the field of industrial catalysis and sensing devices. As an important class of small biological molecules, peptides have the advantages of easy synthesis, excellent biocompatibility, low toxicity, and good water solubility. The peptide–copper complexes exhibit the characteristics of low molecular weight, high tenability, and unique catalytic and photophysical properties. Biosensors with peptide–copper complexes as the signal probes have promising application prospects in environmental monitoring and biomedical analysis and diagnosis. In this review, we discussed the design and application of fluorescent, colorimetric and electrochemical biosensors based on the peptide–copper coordination interaction.

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A novel copper (II) binding peptide for a colorimetric biosensor system design

Cited by 13 publications

References 33 publications

Phage display selection of a Pb(II) specific peptide and its application as a biorecognition unit for colorimetric detection of Pb(II) ions

Phage display selection of a Pb(II) specific peptide and its application as a biorecognition unit for colorimetric detection of Pb(II) ions

Binding stability of peptides to Co–Cr–Mo alloy affects proliferation and differentiation of osteoblast

Progress in the Development of Biosensors Based on Peptide–Copper Coordination Interaction

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