Evidence map›Paper›PMID 38267574›Full record

ArticleThe Journal of antibiotics2024

Precursor-directed biosynthesis and biological activity of tripropeptin Cpip, a new tripropeptin C analog containing pipecolic acid.

Hideki Hashizume, Ryuichi Sawa, Yumiko Kubota, Shinya Adachi, Shigeko Harada, Masayuki Igarashi

Abstract read
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In one paragraph

Article in The Journal of antibiotics, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.7field-weighted citation impact, top 33% of its field
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

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.

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

Who cites it

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Hideki HashizumeLaboratory of Microbiology, Institute of Microbial Chemistry (BIKAKEN), Tokyo, 3-14-23 Kamiosaki, Shinagawa-ku, Tokyo, 141-0021, Japan. hashizumeh@bikaken.or.jp.
Ryuichi SawaLaboratory of Molecular Structure Analysis, Institute of Microbial Chemistry (BIKAKEN), Tokyo, 3-14-23 Kamiosaki, Shinagawa-ku, Tokyo, 141-0021, Japan.ORCID 0000-0002-8190-0195
Yumiko KubotaLaboratory of Molecular Structure Analysis, Institute of Microbial Chemistry (BIKAKEN), Tokyo, 3-14-23 Kamiosaki, Shinagawa-ku, Tokyo, 141-0021, Japan.
Shinya AdachiLaboratory of Molecular Structure Analysis, Institute of Microbial Chemistry (BIKAKEN), Tokyo, 3-14-23 Kamiosaki, Shinagawa-ku, Tokyo, 141-0021, Japan.
Shigeko HaradaLaboratory of Microbiology, Institute of Microbial Chemistry (BIKAKEN), Tokyo, 3-14-23 Kamiosaki, Shinagawa-ku, Tokyo, 141-0021, Japan.
Masayuki IgarashiLaboratory of Microbiology, Institute of Microbial Chemistry (BIKAKEN), Tokyo, 3-14-23 Kamiosaki, Shinagawa-ku, Tokyo, 141-0021, Japan.ORCID 0000-0002-1562-6685
Microbial Chemistry Research Foundation · JP

Funding

MEXT | Japan Society for the Promotion of Science (JSPS) 16K08338MEXT | Japan Society for the Promotion of Science (JSPS) 24710254
6 · The paper itself

Abstract

Tripropeptin C, a non-ribosomal cyclic lipopeptide containing three proline residues, exhibits excellent efficacy in the mouse-methicillin-resistant Staphylococcus aureus septicemia model. Since tripropeptins contain L-prolyl-D-proline and, as a result, are known to form a hairpin structure in proteins, it was of interest to determine whether this substructure contributes to their antibacterial activity. In this study, prolines in tripropeptin C were replaced with pipecolic acid(s) using precursor-directed biosynthesis. Only a new tripropeptin analog, tripropeptin Cpip, which has one L-pipecolic acid in place of L-proline, was isolated. The in vitro antimicrobial activity of the new analog was approximately two to four times weaker activity against Gram-positive bacteria, including drug-resistant species, compared with that of tripropeptin C. These results suggest that the L-prolyl-D-proline substructure plays an important role in the observed potency of tripropeptins.

Indexed as

Inositol PhosphatesMethicillin-Resistant Staphylococcus aureusPipecolic AcidsProstaglandins EAnimalsAnti-Bacterial AgentsLipopeptidesMiceMicrobial Sensitivity TestsProlineAnti-Bacterial AgentsInositol PhosphatesLipopeptidespipecolic acidPipecolic AcidsProlineprostaglandin-inositol cyclic phosphateProstaglandins Etripropeptin C

Identifiers

PMID38267574
OpenAlexW4391173258

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.