Evidence map›Paper›PMID 31941718›Full record

ArticleThe Journal of pharmacology and experimental therapeutics2020

Probing the Assembly of HDL Mimetic, Drug Carrying Nanoparticles Using Intrinsic Fluorescence.

Sangram Raut, Ashwini Garud, Bhavani Nagarajan, Nirupama Sabnis, Alan Remaley, Rafal Fudala, Ignacy Gryczynski, Zygmunt Gryczynski, Sergei V Dzyuba, Julian Borejdo and 1 more

Erratum issuedOpen access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of pharmacology and experimental therapeutics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 51% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Apolipoprotein mimetics in cancer.Seminars in cancer biology · 2021
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 1 institution in 1 country.

Sangram RautDepartments of Physiology and Anatomy (S.R., A.G., B.N., N.S., A.L.) and Microbiology, Immunology and Genetics (R.F., I.G., Z.G., J.B.), UNT Health Science Center, Fort Worth, Texas; National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland (A.R.); and Departments of Physics and Astronomy (Z.G.) and Chemistry and Biochemistry (S.V.D.), Texas Christian University, Fort Worth, Texas.ORCID 0000-0002-1219-3968
Ashwini GarudDepartments of Physiology and Anatomy (S.R., A.G., B.N., N.S., A.L.) and Microbiology, Immunology and Genetics (R.F., I.G., Z.G., J.B.), UNT Health Science Center, Fort Worth, Texas; National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland (A.R.); and Departments of Physics and Astronomy (Z.G.) and Chemistry and Biochemistry (S.V.D.), Texas Christian University, Fort Worth, Texas.
Bhavani NagarajanDepartments of Physiology and Anatomy (S.R., A.G., B.N., N.S., A.L.) and Microbiology, Immunology and Genetics (R.F., I.G., Z.G., J.B.), UNT Health Science Center, Fort Worth, Texas; National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland (A.R.); and Departments of Physics and Astronomy (Z.G.) and Chemistry and Biochemistry (S.V.D.), Texas Christian University, Fort Worth, Texas.ORCID 0000-0002-0432-2846
Nirupama SabnisDepartments of Physiology and Anatomy (S.R., A.G., B.N., N.S., A.L.) and Microbiology, Immunology and Genetics (R.F., I.G., Z.G., J.B.), UNT Health Science Center, Fort Worth, Texas; National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland (A.R.); and Departments of Physics and Astronomy (Z.G.) and Chemistry and Biochemistry (S.V.D.), Texas Christian University, Fort Worth, Texas.
Alan RemaleyDepartments of Physiology and Anatomy (S.R., A.G., B.N., N.S., A.L.) and Microbiology, Immunology and Genetics (R.F., I.G., Z.G., J.B.), UNT Health Science Center, Fort Worth, Texas; National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland (A.R.); and Departments of Physics and Astronomy (Z.G.) and Chemistry and Biochemistry (S.V.D.), Texas Christian University, Fort Worth, Texas.ORCID 0000-0001-5839-7280
Rafal FudalaDepartments of Physiology and Anatomy (S.R., A.G., B.N., N.S., A.L.) and Microbiology, Immunology and Genetics (R.F., I.G., Z.G., J.B.), UNT Health Science Center, Fort Worth, Texas; National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland (A.R.); and Departments of Physics and Astronomy (Z.G.) and Chemistry and Biochemistry (S.V.D.), Texas Christian University, Fort Worth, Texas.
Ignacy GryczynskiDepartments of Physiology and Anatomy (S.R., A.G., B.N., N.S., A.L.) and Microbiology, Immunology and Genetics (R.F., I.G., Z.G., J.B.), UNT Health Science Center, Fort Worth, Texas; National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland (A.R.); and Departments of Physics and Astronomy (Z.G.) and Chemistry and Biochemistry (S.V.D.), Texas Christian University, Fort Worth, Texas.ORCID 0000-0003-1747-9698
Zygmunt GryczynskiDepartments of Physiology and Anatomy (S.R., A.G., B.N., N.S., A.L.) and Microbiology, Immunology and Genetics (R.F., I.G., Z.G., J.B.), UNT Health Science Center, Fort Worth, Texas; National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland (A.R.); and Departments of Physics and Astronomy (Z.G.) and Chemistry and Biochemistry (S.V.D.), Texas Christian University, Fort Worth, Texas.ORCID 0000-0001-8086-2791
Sergei V DzyubaDepartments of Physiology and Anatomy (S.R., A.G., B.N., N.S., A.L.) and Microbiology, Immunology and Genetics (R.F., I.G., Z.G., J.B.), UNT Health Science Center, Fort Worth, Texas; National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland (A.R.); and Departments of Physics and Astronomy (Z.G.) and Chemistry and Biochemistry (S.V.D.), Texas Christian University, Fort Worth, Texas.ORCID 0000-0002-4835-5885
Julian BorejdoDepartments of Physiology and Anatomy (S.R., A.G., B.N., N.S., A.L.) and Microbiology, Immunology and Genetics (R.F., I.G., Z.G., J.B.), UNT Health Science Center, Fort Worth, Texas; National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland (A.R.); and Departments of Physics and Astronomy (Z.G.) and Chemistry and Biochemistry (S.V.D.), Texas Christian University, Fort Worth, Texas.ORCID 0000-0003-4769-5113
Andras LackoDepartments of Physiology and Anatomy (S.R., A.G., B.N., N.S., A.L.) and Microbiology, Immunology and Genetics (R.F., I.G., Z.G., J.B.), UNT Health Science Center, Fort Worth, Texas; National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland (A.R.); and Departments of Physics and Astronomy (Z.G.) and Chemistry and Biochemistry (S.V.D.), Texas Christian University, Fort Worth, Texas andras.lacko@unthsc.edu.ORCID 0000-0001-9168-7802
University of North Texas · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reconstituted high-density lipoprotein (HDL) containing apolipoprotein A-I (Apo A-I) mimics the structure and function of endogenous (human plasma) HDL due to its function and potential therapeutic utility in atherosclerosis, cancer, neurodegenerative diseases, and inflammatory diseases. Recently, a new class of HDL mimetics has emerged, involving peptides with amino acid sequences that simulate the the primary structure of the amphipathic alpha helices within the Apo A-I protein. The findings reported in this communication were obtained using a similar amphiphilic peptide (modified via conjugation of a myristic acid residue at the amino terminal aspartic acid) that self-assembles (by itself) into nanoparticles while retaining the key features of endogenous HDL. The studies presented here involve the macromolecular assembly of the myristic acid conjugated peptide (MYR-5A) into nanomicellar structures and its characterization via steady-state and time-resolved fluorescence spectroscopy. The structural differences between the free peptide (5A) and MYR-5A conjugate were also probed, using tryptophan fluorescence, Fӧrster resonance energy transfer (FRET), dynamic light scattering, and gel exclusion chromatography. To our knowledge, this is the first report of a lipoprotein assembly generated from a single ingredient and without a separate lipid component. The therapeutic utility of these nanoparticles (due to their capablity to incorporate a wide range of drugs into their core region for targeted delivery) was also investigated by probing the role of the scavenger receptor type B1 in this process. SIGNIFICANCE STATEMENT: Although lipoproteins have been considered as effective drug delivery agents, none of these nanoformulations has entered clinical trials to date. A major challenge to advancing lipoprotein-based formulations to the clinic has been the availability of a cost-effective protein or peptide constituent, needed for the assembly of the drug/lipoprotein nanocomplexes. This report of a robust, spontaneously assembling drug transport system from a single component could provide the template for a superior, targeted drug delivery strategy for therapeutics of cancer and other diseases (Counsell and Pohland, 1982).

Indexed as

Amino Acid SequenceBiomimetic MaterialsDrug CarriersLipoproteins, HDLNanoparticlesSpectrometry, FluorescenceDrug CarriersLipoproteins, HDL

Identifiers

PMID31941718
PMCPMC7160862
OpenAlexW2999344662

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.