RNA aptamer binding to polyhistidine-tag

Tsuji, Shoutaro; Tanaka, Taku; Hirabayashi, N; Kato, Shintaro; Akitomi, Joe; Egashira, Hazuki; Waga, Iwao; Ohtsu, Takashi

doi:10.1016/j.bbrc.2009.06.014

Cited by 24 publications

(14 citation statements)

References 14 publications

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“…10). Moreover, it was in a similar molar range when compared with the Kd values reported previously for other His 6 -tag/aptamer complexes [25,33]. (4) 12 g of protein sample purified using H3T aptamer; (5) 12 g of protein sample purified using H3T aptamer/IMAC; (6) 12 g of protein sample purified using IMAC; (7) 12 g of protein sample purified using IMAC/H3T aptamer.…”

Section: Biochemical Analysis Of B1 Aptamersupporting

confidence: 59%

“…In recent years, studies of new His 6 -tag binding ligands based on the nucleic acid aptamers have been presented. Tsuji et al [33] showed an RNA aptamer, which was successfully used to pull down proteins containing the polyhistidine-tag. The results from other studies revealed the possible employment of ssDNA aptamers for the purification of recombinant proteins containing the His 6 -tag [25].…”

Section: Identification Of Sodium Ions-dependent His 3 -Tag Binding Smentioning

confidence: 99%

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Imidazole-free purification of His 3 -tagged recombinant proteins using ssDNA aptamer-based affinity chromatography

Bartnicki

Kowalska

Pels

et al. 2015

Journal of Chromatography A

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Section: Biochemical Analysis Of B1 Aptamersupporting

confidence: 59%

Section: Identification Of Sodium Ions-dependent His 3 -Tag Binding Smentioning

confidence: 99%

Imidazole-free purification of His 3 -tagged recombinant proteins using ssDNA aptamer-based affinity chromatography

Bartnicki

Kowalska

Pels

et al. 2015

Journal of Chromatography A

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“…However, in Hishot display, many different complexes can be formed in exponentially propagating bacteria. In addition, the RNA aptamer used in this study, shot47, has such a small dissociation constant (<3.78 pM) that it is difficult to measure; in fact, the dissociation between the aptamer and the His-tag cannot be detected [14]. Moreover, in this study, we showed that the clones recognizing individual targets were isolated by using Hishot display.…”

Section: Discussionmentioning

confidence: 83%

“…The RNA aptamer, shot47, binds strongly to the His-tag with a low picomolar dissociation constant [14]. Furthermore, shot47 can form a stable complex with His-tagged protein in bacterial lysates.…”

Section: Resultsmentioning

confidence: 99%

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Hishot Display—A New Combinatorial Display for Obtaining Target-Recognizing Peptides

et al. 2013

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Display technologies are procedures used for isolating target-recognizing peptides without using immunized animals. In this study, we describe a new display method, named Hishot display, that uses Escherichia coli and an expression plasmid to isolate target-recognizing peptides. This display method is based on the formation, in bacteria, of complexes between a polyhistidine (His)-tagged peptide including random sequences and the peptide-encoding mRNA including an RNA aptamer against the His-tag. When this system was tested using a sequence encoding His-tagged green fluorescent protein that included an RNA aptamer against the His-tag, the collection of mRNA encoding the protein was dependent on the RNA aptamer. Using this display method and a synthetic library of surrogate single-chain variable fragments consisting of VpreB and Ig heavy-chain variable domains, it was possible to isolate clones that could specifically recognize a particular target (intelectin-1 or tumor necrosis factor-α). These clones were obtained as soluble proteins produced by E. coli, and the purified peptide clones recognizing intelectin-1 could be used as detectors for sandwich enzyme-linked immunosorbent assays. The Hishot display will be a useful method to add to the repertoire of display technologies.

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RNA aptamers selected against yeast cells inhibit Candida albicans biofilm formation in vitro

Bachtiar

Srisawat

2019

MicrobiologyOpen

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Aptamers that bind live bacterial cells have been widely investigated, but their potential to inhibit Candida albicans biofilm formation needs to be further explored. The aims of this study were to evaluate the binding of C. albicans to RNA aptamers and to examine the potential of aptamers to inhibit C. albicans biofilm formation in vitro. In this study, RNA aptamers selected against yeast cells of C. albicans ATCC 10231 were developed using the systematic evolution of ligands by exponential enrichment (SELEX) technique. The binding affinity of the resulting aptamers was then determined by an aptamer‐linked immobilized sorbent assay (ALISA), and a colorimetric (MTT) assay was used to measure the metabolic activity of Candida biofilms. After 11 rounds of SELEX, two candidate aptamers, Ca‐apt‐1 and Ca‐apt‐12, were identified. The Ca‐apt‐1 aptamer also recognized C. albicans isolated from clinical specimens but did not recognize other oral microorganisms (i.e., Streptococcus mutans and Saccharomyces cerevisiae). The ALISA results showed that the binding affinity of these aptamers was comparable to that of an anti‐C. albicans monoclonal antibody. In addition, Ca‐apt‐1 could inhibit biofilm and hyphal formation of C. albicans in vitro, as demonstrated using biofilm assays. This study shows that RNA aptamers could potentially be used in diagnostic and therapeutic applications for C. albicans‐related disease in the future.

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RNA aptamer binding to polyhistidine-tag

Cited by 24 publications

References 14 publications

Imidazole-free purification of His 3 -tagged recombinant proteins using ssDNA aptamer-based affinity chromatography

Imidazole-free purification of His 3 -tagged recombinant proteins using ssDNA aptamer-based affinity chromatography

Hishot Display—A New Combinatorial Display for Obtaining Target-Recognizing Peptides

RNA aptamers selected against yeast cells inhibit Candida albicans biofilm formation in vitro

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