ArticleMolecular biology reports2012
LDP12, a novel cell-permeable peptide derived from L1 capsid protein of the human papillomavirus.
Article in Molecular biology reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed.
- Cell-penetrating peptide-mediated cell entry of H5N1 highly pathogenic avian influenza virus.Scientific reports · 2020Article
- Article
- Advances in intravesical therapy for urinary tract disorders.Expert opinion on drug delivery · 2016Review
- Article
- Coat as a dagger: the use of capsid proteins to perforate membranes during non-enveloped DNA viruses trafficking.Viruses · 2014Review
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We designed a novel cell-permeable peptide, LDP12, from the human papillomavirus L1 capsid protein. In this work, we examined the mechanism of cellular entry by LDP12 and its efficacy as a potential carrier of protein cargoes. The 12-mer peptide linked to FITC freely enters various types of mammalian cells within a few minutes via an endocytic pathway, as its entry is blocked at a low temperature. Several inhibitors which block certain pathway of endocytosis were used to determine which pathway is utilized by LDP12. We found that methyl-β-cyclodextrin specifically blocks LDP12 entry, suggesting that lipid raft-mediated pathway is involved. Intraluminal injection of LDP12-FITC into the mouse uterus shows that this peptide could penetrate the uterine tissue and stay as long as 24 h. Furthermore, LDP12 with a cysteamide group at the C-terminus successfully carries purified protein cargoes into mammalian cells including rat cortical neurons. Collectively, LDP12 could be utilized as a method of protein therapeutics targeting various mammalian cell types.
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Registered trials
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