Evidence map›Paper›PMID 30847433›Full record

ArticleACS omega2019

Nanomedical Relevance of the Intermolecular Interaction Dynamics-Examples from Lysozymes and Insulins.

Ruiyan Zhang, Ning Zhang, Marzieh Mohri, Lisha Wu, Thomas Eckert, Vadim B Krylov, Andrea Antosova, Slavomira Ponikova, Zuzana Bednarikova, Philipp Markart and 15 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS omega, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
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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

25 authors.

Ruiyan ZhangInstitute of Biopharmaceutical Research, Liaocheng University, Liaocheng 252059, P. R. China.
Ning ZhangInstitute of Biopharmaceutical Research, Liaocheng University, Liaocheng 252059, P. R. China.
Marzieh MohriRI-B-NT Research Institute of Bioinformatics and Nanotechnology, Franziusallee 177, 24148 Kiel, Germany.
Lisha WuDepartment of Chemical and Biological Engineering, Chalmers University of Technology, 41296 Gothenburg, Sweden.
Thomas EckertDepartment of Chemistry and Biology, University of Applied Sciences Fresenius, Limburger Str. 2, 65510 Idstein, Germany.
Vadim B KrylovLaboratory of Glycoconjugate Chemistry, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky prospect 47, 119991 Moscow, Russian Federation.
Andrea AntosovaDepartment of Biophysics Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Kosice, Slovakia.
Slavomira PonikovaDepartment of Biophysics Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Kosice, Slovakia.
Zuzana BednarikovaDepartment of Biophysics Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Kosice, Slovakia.
Philipp MarkartMedical Clinic II, Justus-Liebig-University, Klinikstraße 33, 35392 Giessen, Germany.
Andreas GüntherMedical Clinic II, Justus-Liebig-University, Klinikstraße 33, 35392 Giessen, Germany.
Bengt NordenDepartment of Chemical and Biological Engineering, Chalmers University of Technology, 41296 Gothenburg, Sweden.
Martin BilleterDepartment of Chemistry and Molecular Biology, University of Gothenburg, 40530 Gothenburg, Sweden.
Roland SchauerInstitute of Biochemistry, Christian-Albrechts-University, Olshausenstrasse 40, 24098 Kiel, Germany.
Axel J ScheidigInstitute of Zoology, Department of Structural Biology, Christian-Albrechts-University, Am Botanischen Garten 1-9, 24118 Kiel, Germany.
Bhisma N RathaBiomolecular NMR and Drug Design Laboratory, Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), 700054 Kolkata, India.
Anirban BhuniaBiomolecular NMR and Drug Design Laboratory, Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), 700054 Kolkata, India.
Karsten HesseTierarztpraxis Dr. Karsten Hesse, Rathausstraße 16, 35460 Stauffenberg, Germany.
Mushira Abdelaziz EnaniInfectious Diseases Division, Department of Medicine, King Fahad Medical City, P.O. Box 59046, 11525 Riyadh, Kingdom of Saudi Arabia.
Jürgen SteinmeyerLaboratory for Experimental Orthopaedics, Department of Orthopaedics, Justus-Liebig-University, Paul-Meimberg-Str. 3, D-35392 Giessen, Germany.
Athanasios K PetridisNeurochirurgische Klinik, Universität Düsseldorf, Geb. 11.54, Moorenstraße 5, 40255 Düsseldorf, Germany.
Tibor KozarCenter for Interdisciplinary Biosciences, TIP-UPJS, Jesenna 5, 04001 Kosice, Slovakia.
Zuzana GazovaDepartment of Biophysics Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Kosice, Slovakia.
Nikolay E NifantievLaboratory of Glycoconjugate Chemistry, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky prospect 47, 119991 Moscow, Russian Federation.
Hans-Christian SiebertRI-B-NT Research Institute of Bioinformatics and Nanotechnology, Franziusallee 177, 24148 Kiel, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Insulin and lysozyme share the common features of being prone to aggregate and having biomedical importance. Encapsulating lysozyme and insulin in micellar nanoparticles probably would prevent aggregation and facilitate oral drug delivery. Despite the vivid structural knowledge of lysozyme and insulin, the environment-dependent oligomerization (dimer, trimer, and multimer) and associated structural dynamics remain elusive. The knowledge of the intra- and intermolecular interaction profiles has cardinal importance for the design of encapsulation protocols. We have employed various biophysical methods such as NMR spectroscopy, X-ray crystallography, Thioflavin T fluorescence, and atomic force microscopy in conjugation with molecular modeling to improve the understanding of interaction dynamics during homo-oligomerization of lysozyme (human and hen egg) and insulin (porcine, human, and glargine). The results obtained depict the atomistic intra- and intermolecular interaction details of the homo-oligomerization and confirm the propensity to form fibrils. Taken together, the data accumulated and knowledge gained will further facilitate nanoparticle design and production with insulin or lysozyme-related protein encapsulation.

Identifiers

PMID30847433
PMCPMC6398350

What Socratic 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 Socratic graph.