Evidence map›Paper›PMID 40531453›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2025

Diol as a New Pantetheine Surrogate for Chemoenzymatic Synthesis of Cyclic Peptides via Nonribosomal Peptide Cyclases.

Kei Fujita, Rintaro Ichihara, Masakazu Kobayashi, Kenichi Matsuda, Toshiyuki Wakimoto

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Article in Methods in molecular biology (Clifton, N.J.), 2025. 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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0citing papers 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

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

5 authors.

Kei FujitaFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Rintaro IchiharaFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Masakazu KobayashiFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Kenichi MatsudaFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan. kematsuda@pharm.hokudai.ac.jp.
Toshiyuki WakimotoFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan. wakimoto@pharm.hokudai.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nonribosomal peptide cyclases possess enormous biocatalytic potential for cyclizing peptides, including those shorter than ten residues. However, N-acetylcysteamine (SNAC) or related low molecular weight thiol leaving groups, which have traditionally been used as surrogates for a pantetheine group on the substrate C-terminus, necessitate a labor-intensive process to prepare the substrate for cyclases. Our group recently established a faster, automation-compatible synthetic method for cyclase substrates, using ethylene glycol (EG) as a new pantetheine surrogate. This approach significantly streamlines substrate preparation while maintaining cyclization efficiency. In this chapter, we describe the synthetic pathway for the solid-phase peptide synthesis of EG-functionalized peptides, followed by enzymatic cyclization using nonribosomal peptide cyclases.

Indexed as

PantetheinePeptides, CyclicPeptide SynthasesCyclizationEthylene GlycolSolid-Phase Synthesis TechniquesEthylene Glycolnon-ribosomal peptide synthasePantetheinePeptides, CyclicPeptide SynthasesChemo-enzymatic synthesisCyclic peptidesEthylene glycolNonribosomal peptide synthesisPeptide cyclase

Identifiers

PMID40531453

What OpenQuestion holds

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Registered trials

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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.