Evidence map›Paper›PMID 33810400›Full record

ArticleBiomolecules2021

Structure and Location of Protein Sites Binding Self-Associated Congo Red Molecules with Intercalated Drugs as Compact Ligands-Theoretical Studies.

Ptak-Kaczor Magdalena, Kwiecińska Klaudia, Korchowiec Jacek, Chłopaś Katarzyna, Banach Mateusz, Roterman Irena, Jagusiak Anna

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 45% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

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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

7 authors at 1 institution in 1 country.

Ptak-Kaczor MagdalenaDepartment of Bioinformatics and Telemedicine, Faculty of Medicine, Jagiellonian University Medical College, Medyczna 7, 30-688 Krakow, Poland.
Kwiecińska KlaudiaDepartment of Theoretical Chemistry, Faculty of Chemistry, Jagiellonian University, K. Gumiński, Gronostajowa 2, 30-387 Kraków, Poland.
Korchowiec JacekDepartment of Theoretical Chemistry, Faculty of Chemistry, Jagiellonian University, K. Gumiński, Gronostajowa 2, 30-387 Kraków, Poland.
Chłopaś KatarzynaFaculty of Medicine, Chair of Medical Biochemistry, Jagiellonian University Medical College, Kopernika 7, 31-034 Krakow, Poland.
Banach MateuszDepartment of Bioinformatics and Telemedicine, Faculty of Medicine, Jagiellonian University Medical College, Medyczna 7, 30-688 Krakow, Poland.ORCID 0000-0003-1806-9877
Roterman IrenaDepartment of Bioinformatics and Telemedicine, Faculty of Medicine, Jagiellonian University Medical College, Medyczna 7, 30-688 Krakow, Poland.
Jagusiak AnnaFaculty of Medicine, Chair of Medical Biochemistry, Jagiellonian University Medical College, Kopernika 7, 31-034 Krakow, Poland.ORCID 0000-0002-4440-5160
Jagiellonian University · PL

Funding

National Science Centre, Poland 2016/21/D/NZ1/02763
6 · The paper itself

Abstract

In the search for new carriers capable of transporting toxic drugs to a target, particular attention has been devoted to supramolecular systems with a ribbon-like micellar structure of which Congo red is an example. A special promise of the possible use of such systems for directing drugs to a target emerges from their particular affinity to immune complexes and as an independent property, binding many organic compounds including drugs by intercalation. Serum albumin also appeared able to bind micellar particles of such systems. It may protect them against dilution in transport. The mathematical tool, which relies on analysis of the distribution of polarity and hydrophobicity in protein molecules (fuzzy oil drop model), has been used to find the location of binding area in albumin as well as anchorage site for Congo red in heated IgG light chain used as a model presenting immunoglobulin-like structures. Results confirm the suggested formerly binding site of Congo red in V domain of IgG light chain and indicated the cleft between pseudo-symmetric domains of albumin as the area of attachment for the dye.

Indexed as

AlbuminsBinding SitesCongo RedHumansHydrophobic and Hydrophilic InteractionsImmunoglobulin Light ChainsIntercalating AgentsProtein BindingProteinsProtein Structure, TertiaryStatic ElectricityAlbuminsCongo RedImmunoglobulin Light ChainsIntercalating AgentsProteinsalbuminBence-Jones proteindoxorubicindrug carrierfuzzy oil drop modelhydrophobic corehydrophobicitylight chain of IgG

Identifiers

PMID33810400
PMCPMC8065709
OpenAlexW3140137655

What OpenQuestion holds

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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.