ArticleAdvanced biosystems2018
Cell-penetrating Chaperone Peptide Prevents Protein Aggregation And Protects Against Cell Apoptosis.
Article in Advanced biosystems, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Improvement of Adeno-Associated Virus (AAV)-Based Technologies by Cell-Penetrating Penta-Peptides (CPP5s).Pharmaceutics · 2026Review
- Mechanisms contributing to inhibition of retinal ganglion cell death by cell permeable peptain-1 under glaucomatous stress.Cell death discovery · 2024Article
- Therapeutic Potential of α-Crystallins in Retinal Neurodegenerative Diseases.Antioxidants (Basel, Switzerland) · 2021Review
- Irradiation effect of a submillimeter wave from 420 GHz gyrotron on amyloid peptides in vitro.Biomedical optics express · 2020Article
- Spatiotemporal changes in the human lens proteome: Critical insights into long-lived proteins.Progress in retinal and eye research · 2020Review
- Development of a brain-permeable peptide nanofiber that prevents aggregation of Alzheimer pathogenic proteins.PloS one · 2020Article
- Systemically administered peptain-1 inhibits retinal ganglion cell death in animal models: implications for neuroprotection in glaucoma.Cell death discovery · 2019Article
- Small Heat Shock Proteins, Big Impact on Protein Aggregation in Neurodegenerative Disease.Frontiers in pharmacology · 2019Review
- Suppression of aggregate and amyloid formation by a novel intrinsically disordered region in metazoan Hsp110 chaperones.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Many of the newly discovered therapeutic peptides and molecules are limited by their inability to cross the cell membrane. In the present study we employed a cell penetrating peptide (CPP), VPTLK, derived from Ku70 protein, to facilitate the entry of a mini-chaperone across the cell membrane. Our previous studies suggest that the mini-chaperone peptide representing the chaperone site in αA-crystallin, which can inhibit protein aggregation associated with proteopathies, has therapeutic potential. We have prepared a synthetic mini-chaperone by fusing the VPTLK sequence to N-terminus of mini-chaperone (FVIFLDVKHFSPEDLTVKGRD) to get VPTLKFVIFLDVKHFSPEDLTVKGRD peptide, which we call "CPPGRD." The amino acids, GRD, were added to increase the solubility of the peptide. The chaperone-like function of CPPGRD was measured using unfolding conditions for alcohol dehydrogenase and α-lactalbumin. The anti-apoptotic action of the peptide chaperone was evaluated using H
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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.