Evidence map›Paper›PMID 33781808›Full record

ArticleJournal of controlled release : official journal of the Controlled Release Society2021

Self-assembled elastin-like polypeptide fusion protein coacervates as competitive inhibitors of advanced glycation end-products enhance diabetic wound healing.

Hwan June Kang, Suneel Kumar, Arielle D'Elia, Biraja Dash, Vikas Nanda, Henry C Hsia, Martin L Yarmush, François Berthiaume

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of controlled release : official journal of the Controlled Release Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
6.2field-weighted citation impact, top 2% 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

37 citing papers in PubMed, 73 citations in OpenAlex.

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  16. Unveiling the therapeutic journey of snail mucus in diabetic wound care.Naunyn-Schmiedeberg's archives of pharmacology · 2025
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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

8 authors at 2 institutions in 1 country.

Hwan June KangDepartment of Biomedical Engineering, Rutgers University, Piscataway, NJ 08854, USA.
Suneel KumarDepartment of Biomedical Engineering, Rutgers University, Piscataway, NJ 08854, USA.
Arielle D'EliaDepartment of Biomedical Engineering, Rutgers University, Piscataway, NJ 08854, USA.
Biraja DashDepartment of Surgery (Plastic), Yale School of Medicine, New Haven, CT 06510, USA.
Vikas NandaDepartment of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, NJ 08854, USA.
Henry C HsiaDepartment of Surgery (Plastic), Yale School of Medicine, New Haven, CT 06510, USA.
Martin L YarmushDepartment of Biomedical Engineering, Rutgers University, Piscataway, NJ 08854, USA.
François BerthiaumeDepartment of Biomedical Engineering, Rutgers University, Piscataway, NJ 08854, USA. Electronic address: fberthia@soe.rutgers.edu.
Rutgers, The State University of New Jersey · USYale University · US

Funding

Multifunctional Nanoparticles Containing sRAGE Potentiated Bioactive Peptides for Wound HealingR21EB021570 · NIBIB · RUTGERS, THE STATE UNIV OF N.J. · PI BERTHIAUME, FRANCOIS, YARMUSH, MARTIN L · 2016 to 2017
$442k
NIBIB NIH HHS R21 EB021570
6 · The paper itself

Abstract

Chronic and non-healing skin wounds are some of the most significant complications in patients with advanced diabetes. A contributing mechanism to this pathology is the non-enzymatic glycation of proteins due to hyperglycemia, leading to the formation of advanced glycation end products (AGEs). AGEs bind to the receptor for AGEs (RAGE), which triggers pro-inflammatory signals that may inhibit the proliferative phase of wound healing. Soluble forms of RAGE (sRAGE) may be used as a competitive inhibitor of AGE-mediated signaling; however, sRAGE is short-lived in the highly proteolytic wound environment. We developed a recombinant fusion protein containing the binding domain of RAGE (vRAGE) linked to elastin-like polypeptides (ELPs) that self-assembles into coacervates at around 30-31 °C. The coacervate size was concentration and temperature-dependent, ranging between 500 and 1600 nm. vRAGE-ELP reversed several AGE-mediated changes in cultured human umbilical vein endothelial cells, including a decrease in viable cell number, an increase in levels of reactive oxygen species (ROS), and an increased expression of the pro-inflammatory marker, intercellular adhesion molecule-1 (ICAM-1). vRAGE-ELP was stable in elastase in vitro for 7 days. When used in a single topical application on full-thickness excisional skin wounds in diabetic mice, wound closure was accelerated, with 90% and 100% wound closure on post-wounding days 28 and 35, respectively, compared to 62% and 85% on the same days in animals treated with vehicle control, consisting of ELP alone. This coacervate system topically delivering a competitive inhibitor of AGEs has potential for the treatment of diabetic wounds.

Indexed as

Diabetes Mellitus, ExperimentalElastinAnimalsHumansMicePeptidesReceptor for Advanced Glycation End ProductsSkinWound HealingElastinPeptidesReceptor for Advanced Glycation End ProductsAdvanced glycation end-productChronic skin woundsDiabetic foot ulcerElastin-like polypeptideSelf-assembled coacervates

Identifiers

PMID33781808
PMCPMC10927318
OpenAlexW3141185320

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.