Characterization of the Binding Behavior of Specific Cobalt and Nickel Ion-Binding Peptides Identified by Phage Surface Display

In recent years, the application focus of phage surface display (PSD) technology has been extended to the identification of metal ion-selective peptides. In previous studies, two phage clones—a nickel-binding one with the peptide motif CNAKHHPRCGGG and a cobalt-binding one with the peptide motif CTQ...

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Published in:Separations 2022-11, Vol.9 (11), p.354
Main Authors: Matys, Sabine, Morawietz, Lisa-Marie, Lederer, Franziska, Pollmann, Katrin
Format: Article
Language:English
Subjects:
Affinity
Bacteriophages
Binding
biopanning
Buffers
Chemical elements
Chemical properties
Cloning
Cobalt
Experiments
isothermal titration calorimetry
metal-binding peptides
Nickel
Peptides
phage surface display
Phages
Physiological aspects
Protein binding
Protein research
Salt
Selectivity
Software
Spectrum analysis
Titration calorimetry
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cited_by cdi_FETCH-LOGICAL-c452t-6d0d603d58eb322205255124f1245df174d2e91c6ef5a3cb8e389cf0d62139853
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container_issue 11
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creator Matys, Sabine
Morawietz, Lisa-Marie
Lederer, Franziska
Pollmann, Katrin
description In recent years, the application focus of phage surface display (PSD) technology has been extended to the identification of metal ion-selective peptides. In previous studies, two phage clones—a nickel-binding one with the peptide motif CNAKHHPRCGGG and a cobalt-binding one with the peptide motif CTQMLGQLCGGG—were isolated, and their binding ability to metal-loaded NTA agarose beads was investigated. Here, the free cyclic peptides are characterized by UV/VIS spectroscopy with respect to their binding capacity for the respective target ion and in crossover experiments for the other ion by isothermal titration calorimetry (ITC) in different buffer systems. This revealed differences in selectivity and affinity. The cobalt-specific peptide is very sensitive to different buffers; it has a 20-fold higher affinity for cobalt and nickel under suitable conditions. The nickel-specific peptide binds more moderately and robustly in different buffers but only selectively to nickel.
doi_str_mv 10.3390/separations9110354
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subjects Affinity
Bacteriophages
Binding
biopanning
Buffers
Chemical elements
Chemical properties
Cloning
Cobalt
Experiments
isothermal titration calorimetry
metal-binding peptides
Nickel
Peptides
phage surface display
Phages
Physiological aspects
Protein binding
Protein research
Salt
Selectivity
Software
Spectrum analysis
Titration calorimetry
title Characterization of the Binding Behavior of Specific Cobalt and Nickel Ion-Binding Peptides Identified by Phage Surface Display
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