Evidence map›Paper›PMID 38357956›Full record

ArticleCurrent cancer drug targets2024

Stabilizing Scaffold for Short Peptides Based on Knottins.

Evgenii Beloborodov, Elena Iurova, Dmitrii Sugak, Eugenia Rastorgueva, Evgeniya Pogodina, Aleksandr Fomin, Denis Viktorov, Sergei Slesarev, Yury Saenko

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Article in Current cancer drug targets, 2024. 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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1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

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0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

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5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Evgenii BeloborodovLaboratory of Research and Development of Peptide Drugs and Vaccines, S.P. Kapitsa Technological Research Institute, Ulyanovsk State University, Ulyanovsk, Russia.
Elena IurovaLaboratory of Research and Development of Peptide Drugs and Vaccines, S.P. Kapitsa Technological Research Institute, Ulyanovsk State University, Ulyanovsk, Russia.
Dmitrii SugakLaboratory of Research and Development of Peptide Drugs and Vaccines, S.P. Kapitsa Technological Research Institute, Ulyanovsk State University, Ulyanovsk, Russia.
Eugenia RastorguevaLaboratory of Research and Development of Peptide Drugs and Vaccines, S.P. Kapitsa Technological Research Institute, Ulyanovsk State University, Ulyanovsk, Russia.
Evgeniya PogodinaLaboratory of Research and Development of Peptide Drugs and Vaccines, S.P. Kapitsa Technological Research Institute, Ulyanovsk State University, Ulyanovsk, Russia.
Aleksandr FominLaboratory of Research and Development of Peptide Drugs and Vaccines, S.P. Kapitsa Technological Research Institute, Ulyanovsk State University, Ulyanovsk, Russia.
Denis ViktorovLaboratory of Research and Development of Peptide Drugs and Vaccines, S.P. Kapitsa Technological Research Institute, Ulyanovsk State University, Ulyanovsk, Russia.
Sergei SlesarevDepartment of Biology, Ecology and Natural Resources Management, Faculty of Ecology, Ulyanovsk State University, Ulyanovsk, Russia.
Yury SaenkoLaboratory of Research and Development of Peptide Drugs and Vaccines, S.P. Kapitsa Technological Research Institute, Ulyanovsk State University, Ulyanovsk, Russia.
Ulyanovsk State University · RU

Funding

Ministry of Education and Science of the Russian Federation ,123020700216 (FEUF-2023-0004),123020700216,123020700216,123020700216,123020700216 (FEUF-2023-0004),123020700216 (FEUF-2023-0004)
6 · The paper itself

Abstract

backgroundBombesin (BBN) is a short peptide with a high affinity for receptors that are expressed on the surface of various types of cancer cells. However, a full length BBN molecule has low

objectiveIn our study, we propose the use of peptide toxins, derived from animal and plant toxins, as scaffold molecules to enhance the bioavailability and stability of bombesin. These peptides possess a unique structure known as an inhibitory cystine knot.

methodsWe synthesized structures in which short bombesin was incorporated into various domains of arthropod and plant toxins using solid-phase peptide synthesis. The stability under different conditions was assessed through high-performance liquid chromatography, and binding to cell cultures expressing the bombesin receptor was analyzed. Additionally, toxicity to cell cultures was evaluated using fluorescence microscopy.

resultsThe data obtained demonstrated that placing the short peptide between the first and second cysteine residues in arachnid toxins results in increased

conclusionArachnid toxins with an inhibitory cystine knot can be considered as a scaffold for increasing the stability of therapeutic peptides.

Indexed as

BombesinAnimalsCystine-Knot MiniproteinsHumansPeptidesBombesinCystine-Knot MiniproteinsPeptidesBombesincancerinhibitory cystine knotpeptide toxinproteins.stability

Identifiers

PMID38357956
OpenAlexW4391840451

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