Evidence map›Paper›PMID 38427104›Full record

ArticleAmino acids2024

Applications of biaryl cyclization in the synthesis of cyclic enkephalin analogs with a highly restricted flexibility.

Maria Różanowska, Gabriela Szczupaj, Michał Nowakowski, Priyadharshni Rajagopal, Piotr F J Lipiński, Joanna Matalińska, Aleksandra Misicka, Marek Lisowski, Łukasz Jaremko, Mariusz Jaremko

Open access · goldAbstract read
In one paragraph

Article in Amino acids, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

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

10 authors at 5 institutions in 2 countries.

Maria RóżanowskaFaculty of Chemistry, University of Wrocław, Wrocław, Poland. maria.rozanowska2@uwr.edu.pl.
Gabriela SzczupajFaculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw, Warsaw, Poland.
Michał NowakowskiFaculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw, Warsaw, Poland.
Priyadharshni RajagopalBioscience Program, Division of Biological and Environmental Sciences and Engineering (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.
Piotr F J LipińskiDepartment of Neuropeptides, Mossakowski Medical Research Institute, Polish Academy of Sciences, Warsaw, Poland.
Joanna MatalińskaDepartment of Neuropeptides, Mossakowski Medical Research Institute, Polish Academy of Sciences, Warsaw, Poland.
Aleksandra MisickaDepartment of Neuropeptides, Mossakowski Medical Research Institute, Polish Academy of Sciences, Warsaw, Poland.
Marek LisowskiFaculty of Chemistry, University of Wrocław, Wrocław, Poland.
Łukasz JaremkoBioscience Program, Division of Biological and Environmental Sciences and Engineering (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.
Mariusz JaremkoBioscience Program, Division of Biological and Environmental Sciences and Engineering (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia. mariusz.jaremko@kaust.edu.sa.
King Abdullah University of Science and Technology · SAMossakowski Medical Research Institute, Polish Academy of Sciences · PLUniversity of Warsaw · PLUniversity of Wrocław · PLPolish Academy of Sciences · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A series of 10 cyclic, biaryl analogs of enkephalin, with Tyr or Phe residues at positions 1 and 4, were synthesized according to the Miyaura borylation and Suzuki coupling methodology. Biaryl bridges formed by side chains of the two aromatic amino acid residues are of the meta-meta, meta-para, para-meta, and para-para configuration. Conformational properties of the peptides were studied by CD and NMR. CD studies allowed only to compare conformations of individual peptides while NMR investigations followed by XPLOR calculations provided detailed information on their conformation. Reliability of the XPLOR calculations was confirmed by quantum chemical ones performed for one of the analogs. No intramolecular hydrogen bonds were found in all the peptides. They are folded and adopt the type IV β-turn conformation. Due to a large steric strain, the aromatic carbon atoms forming the biaryl bond are distinctly pyramidalized. Seven of the peptides were tested in vitro for their affinity for the µ-opioid receptor.

Indexed as

EnkephalinsPeptides, CyclicCyclizationProtein ConformationReproducibility of ResultsEnkephalinsPeptides, CyclicBiaryl bridges in peptidesCDCyclizationMiyaura–Suzuki reactionMolecular dockingNMR

Identifiers

PMID38427104
PMCPMC10907494
OpenAlexW4392387175

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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.