Evidence map›Paper›PMID 27603918›Full record

ArticleAnalytical chemistry2016

Thermoresponsive Collagen/Cell Penetrating Hybrid Peptide as Nanocarrier in Targeting-Free Cell Selection and Uptake.

Myungeun Oh, Chloe Hu, Selina F Urfano, Merlyn Arostegui, Katarzyna Slowinska

Abstract read
In one paragraph

Article in Analytical chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Hybrid peptides as platform for synchronized combination therapy.Colloids and surfaces. B, Biointerfaces · 2023
    Article
  2. Article
  3. 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

5 authors.

Myungeun OhDepartment of Chemistry and Biochemistry, California State University Long Beach , Long Beach, California 90840, United States.
Chloe HuDepartment of Chemistry and Biochemistry, California State University Long Beach , Long Beach, California 90840, United States.
Selina F UrfanoDepartment of Chemistry and Biochemistry, California State University Long Beach , Long Beach, California 90840, United States.
Merlyn ArosteguiDepartment of Chemistry and Biochemistry, California State University Long Beach , Long Beach, California 90840, United States.
Katarzyna SlowinskaDepartment of Chemistry and Biochemistry, California State University Long Beach , Long Beach, California 90840, United States.

Funding

CSULB Building Biomedical Research Program: Overall ComponentUL1GM118979 · NIGMS · CALIFORNIA STATE UNIVERSITY LONG BEACH · PI CHUN, CHI-AH, DILLON, JESSE · 2015 to 2023
$20.7M
CSULB Building Biomedical Research Program: Student Training CoreTL4GM118980 · NIGMS · CALIFORNIA STATE UNIVERSITY LONG BEACH · PI CHUN, CHI-AH, DILLON, JESSE · 2015 to 2023
$12.3M
CSULB Building Biomedical Research Program: Research Enrichment CoreRL5GM118978 · NIGMS · CALIFORNIA STATE UNIVERSITY LONG BEACH · PI CHUN, CHI-AH, DILLON, JESSE · 2015 to 2023
$7.3M
Rigid-rod Peptides as Nanocarriers for Delivery of Cancer DrugsSC3GM099594 · NIGMS · CALIFORNIA STATE UNIVERSITY LONG BEACH · PI SLOWINSKA, KATARZYNA · 2012 to 2021
$872k
NIGMS NIH HHS RL5 GM118978NIGMS NIH HHS SC3 GM099594NIGMS NIH HHS TL4 GM118980NIGMS NIH HHS UL1 GM118979
6 · The paper itself

Abstract

The effective delivery of therapeutics and imaging agents to a selected group of cells has been at the forefront of biomedical research. Unfortunately, the identification of the unique cell surface targets for cell selection remains a major challenge, particularly if cells within the selected group are not identical. Here we demonstrate a novel approach to cell section relying on a thermoresponsive peptide-based nanocarrier. The hybrid peptide containing cell-penetrating peptide (CPP) and collagen (COLL) domains is designed to undergo coil-to-helix transition (folding) below physiological temperature. Because only the helical form undergoes effective internalization by the cells, this approach allows effective temperature-discriminate cellular uptake. The cells selected for uptake are locally cooled, thus enabling the carrier to fold and subsequently internalize. Our approach demonstrates a generic method as selected cells could differ from the adjacent cells or could belong to the same cell population. The method is fast (<15 min) and selective; over 99.6% of cells in vitro internalized the peptide carrier at low temperatures (15 °C), while less than 0.2% internalized at 37 °C. In vivo results confirm the high selectivity of the method. The potential clinical applications in mixed cell differentiation carcinoma, most frequently encountered in breast and ovarian cancer, are envisioned.

Indexed as

TemperatureAnimalsCell-Penetrating PeptidesCells, CulturedCollagenDrug CarriersMiceMicroscopy, FluorescenceNanoparticlesNIH 3T3 CellsOligochaetaOptical ImagingCell-Penetrating PeptidesCollagenDrug Carriers

Identifiers

PMID27603918
PMCPMC5177025

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.