ArticleRSC advances2026
Identification of perrhenate-binding peptides by phage display.
Article in RSC advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Authors and funding
5 authors.
Funding
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Abstract
Pertechnetate is the most stable and highly environmentally mobile form of the radioactive element technetium. To explore the ability of peptides to remove this molecule from aqueous solutions, a phage display library was biopanned against immobilized perrhenate, a nonradioactive analog of pertechnetate. Six unique peptides were identified from the screen and their ability to bind perrhenate, both free in solution and immobilized on a solid support, was explored. It was found that the peptides, particularly when immobilized, were able to remove perrhenate from aqueous solutions, and despite not being screened for selectivity, demonstrated some preference for perrhenate over other anions such as chromate and nitrite. These results demonstrate the feasibility of using engineered biological systems for remediation of pertechnetate in the environment.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.