Designed Cell-Penetrating Peptide Constructs for Inhibition of Pathogenic Protein Self-Assembly.
Designed Cell-Penetrating Peptide Constructs for Inhibition of Pathogenic Protein Self-Assembly.
Where did the research take place?
The study site has not been established. Author addresses may differ from where the research occurred.
Abu Dhabi, AE · Author affiliation
Biology Program, Division of Science, New York University Abu Dhabi, Saadiyat Island Campus, Abu Dhabi P.O. Box 129188, United Arab Emirates.Location evidence
IS · Author affiliation · country only
Biology Program, Division of Science, New York University Abu Dhabi, Saadiyat Island Campus, Abu Dhabi P.O. Box 129188, United Arab Emirates.Location evidence
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Original abstract
Peptides possess a number of pharmacologically desirable properties, including greater chemical diversity than other biomolecule classes and the ability to selectively bind to specific targets with high potency, as well as biocompatibility, biodegradability, and ease and low cost of production. Consequently, there has been considerable interest in developing peptide-based therapeutics, including amyloid inhibitors. However, a major hindrance to the successful therapeutic application of peptides is their poor delivery to target tissues, cells or subcellular organelles. To overcome these issues, recent efforts have focused on engineering cell-penetrating peptide (CPP) antagonists of amyloidogenesis, which combine the attractive intrinsic properties of peptides with potent therapeutic effects (i.e., inhibition of amyloid formation and the associated cytotoxicity) and highly efficient delivery (to target tissue, cells, and organelles). This review highlights some promising CPP constructs designed to target amyloid aggregation associated with a diverse range of disorders, including Alzheimer's disease, transmissible spongiform encephalopathies (or prion diseases), Parkinson's disease, and cancer.