ArticlePloS one2014
Elucidation of the interaction mechanism with liposomes of gH625-peptide functionalized dendrimers.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- Article
- Application of Dendrimers for Treating Parasitic Diseases.Pharmaceutics · 2021Review
- Peptides and Dendrimers: How to Combat Viral and Bacterial Infections.Pharmaceutics · 2021Review
- Tailoring Uptake Efficacy of HSV-1 gD Derived Carrier Peptides.Biomolecules · 2020Article
- Biophysical Correlates on the Composition, Functionality, and Structure of Dendrimer-Liposome Aggregates.ACS omega · 2018Article
- Enhanced uptake of gH625 by blood brain barrier compared to liver in vivo: characterization of the mechanism by an in vitro model and implications for delivery.Scientific reports · 2018Article
- Membranotropic peptides mediating viral entry.Peptide science (Hoboken, N.J.) · 2018Review
- Function Oriented Molecular Design: Dendrimers as Novel Antimicrobials.Molecules (Basel, Switzerland) · 2017Review
- Dimerization in tailoring uptake efficacy of the HSV-1 derived membranotropic peptide gH625.Scientific reports · 2017Article
- Article
- Membranotropic Cell Penetrating Peptides: The Outstanding Journey.International journal of molecular sciences · 2015Review
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have demonstrated that amide-based dendrimers functionalized with the membrane-interacting peptide gH625 derived from the herpes simplex virus type 1 (HSV-1) envelope glycoprotein H enter cells mainly through a non-active translocation mechanism. Herein, we investigate the interaction between the peptide-functionalized dendrimer and liposomes composed of PC/Chol using fluorescence spectroscopy, isothermal titration calorimetry, and surface plasmon resonance to get insights into the mechanism of internalization. The affinity for the membrane bilayer is very high and the interaction between the peptide-dendrimer and liposomes took place without evidence of pore formation. These results suggest that the presented peptidodendrimeric scaffold may be a promising material for efficient drug delivery.
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Registered trials
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.