Evidence map›Paper›PMID 33502824›Full record

ArticleMacromolecular bioscience2021

Chemically-Induced Cross-Linking of Peptidic Fibrils for Scaffolding Polymeric Particles and Macrophages.

Jennifer M Armen, Nathan R Schueller, Ketki Y Velankar, Nevil Abraham, Rachelle N Palchesko, Yong Fan, Wilson S Meng, Ellen S Gawalt

Open access · greenAbstract read
In one paragraph

Article in Macromolecular bioscience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 50% 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. Article
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

8 authors at 3 institutions in 1 country.

Jennifer M ArmenDepartment of Chemistry and Biochemistry, Duquesne University, Pittsburgh, PA, 15282, USA.ORCID 0000-0002-8033-6203
Nathan R SchuellerGraduate School of Pharmaceutical Sciences, Duquesne University, Pittsburgh, PA, 15282, USA.ORCID 0000-0001-6609-2153
Ketki Y VelankarGraduate School of Pharmaceutical Sciences, Duquesne University, Pittsburgh, PA, 15282, USA.ORCID 0000-0003-4189-754X
Nevil AbrahamGraduate School of Pharmaceutical Sciences, Duquesne University, Pittsburgh, PA, 15282, USA.
Rachelle N PalcheskoDepartment of Biomedical Engineering, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.ORCID 0000-0001-7101-2496
Yong FanCellular Therapeutics Institute, Allegheny-Singer Research Institute, Allegheny Health Network, Pittsburgh, PA, 15202, USA.
Wilson S MengThe McGowan Institute for Regenerative Medicine, University of Pittsburgh, Pittsburgh, PA, 15212, USA.ORCID 0000-0003-2575-2260
Ellen S GawaltDepartment of Chemistry and Biochemistry, Duquesne University, Pittsburgh, PA, 15282, USA.ORCID 0000-0002-9061-3163
Duquesne University · USAllegheny Health Network · USUniversity of Pittsburgh · US

Funding

Induction of allogeneic tolerance with bioengineered thymus organoidsR01AI123392 · NIAID · ALLEGHENY-SINGER RESEARCH INSTITUTE · PI FAN, YONG · 2016 to 2019
$1.5M
DEVELOPMENT OF A REGULATORY T CELL MIMETIC FOR TOLERANCE INDUCTION IN SKIN TRANSPLANTATIONR21AI139828 · NIAID · DUQUESNE UNIVERSITY · PI MENG, WILSON S · 2019 to 2020
$378k
NIAID NIH HHS R01 AI123392NIAID NIH HHS R21 AI139828
6 · The paper itself

Abstract

EAK16-II (EAK) is a self-assembling peptide (SAP) that forms β-sheets and β-fibrils through ionic-complementary interactions at physiological ionic strengths. The soft materials can be injected in vivo, creating depots of drugs and cells for rendering pharmacological and biological actions. The scope of the applications of EAK is sought to extend to tissues through which the flow of extracellular fluid tends to be limited. In such anatomical locales the rate and extent of the fibrilization are limited insofar as drug delivery and cellular scaffolding would be impeded. A method is generated utilizing a carbodiimide cross-linker by which EAK fibrils are pre-assembled yet remain injectable soft materials. It is hypothesized that the resulting de novo covalent linkages enhance the stacking of the β-sheet bilayers, thereby increasing the lengths of the fibrils and the extent of their cross-linking, as evidenced in Diffuse Reflectance Infrared Fourier Transform (DRIFT) spectroscopy, scanning electron microscopy, and atomic force microscopy analyses. The cross-linked EAK (clEAK) retains polymeric microspheres with an average diameter of 1 µm. Macrophages admixed with clEAK remain viable and do not produce the inflammatory mediator interleukin-1β. These results indicate that clEAK should be investigated further as a platform for delivering particles and cells in vivo.

Indexed as

AnimalsBiocompatible MaterialsCarboxylic AcidsCross-Linking ReagentsDrug Delivery SystemsHydrogelsInterleukin-10Lipid BilayersMacrophagesMicroscopy, Atomic ForceMicroscopy, Electron, ScanningMicrospheresPeptidesPolymersProtein Conformation, beta-StrandProtein Structure, SecondaryBiocompatible MaterialsCarboxylic AcidsCross-Linking ReagentsHydrogelsIL10 protein, humanInterleukin-10Lipid BilayersPeptidesPolymerscell encapsulationEAK16-IIhydrogelsself-assembling peptides

Identifiers

PMID33502824
PMCPMC9578542
OpenAlexW3126049814

What OpenQuestion holds

Textmetadata
LicenceTDM
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.