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Cell-Penetrating Peptides with Unexpected Anti-Amyloid Properties
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0003-0905-7911
Stockholm University, Faculty of Humanities, Department of Archaeology and Classical Studies. CellPept Sweden AB, Sweden.ORCID iD: 0000-0001-6836-5610
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. CellPept Sweden AB, Sweden.ORCID iD: 0000-0003-2187-1537
Number of Authors: 32022 (English)In: Pharmaceutics, ISSN 1999-4923, E-ISSN 1999-4923, Vol. 14, no 4, article id 823Article, review/survey (Refereed) Published
Abstract [en]

Cell-penetrating peptides (CPPs) with sequences derived originally from a prion protein (PrP) have been shown to exhibit both anti-prion and anti-amyloid properties particularly against prion proteins and the amyloid-β (Aβ) peptide active in Alzheimer’s disease. These disease-modifying properties are so far observed in cell cultures and in vitro. The CPP sequences are composed of a hydrophobic signal sequence followed by a highly positively charged hexapeptide segment. The original signal sequence of the prion protein can be changed to the signal sequence of the NCAM1 protein without losing the anti-prion activity. Although the detailed molecular mechanisms of these CPP peptides are not fully understood, they do form amyloid aggregates by themselves, and molecular interactions between the CPPs and PrP/Aβ can be observed in vitro using various spectroscopic techniques. These initial intermolecular interactions appear to re-direct the aggregation pathways for prion/amyloid formation to less cell-toxic molecular structures (i.e., co-aggregates), which likely is why the disease-inducing PrP/Aβ aggregation is counteracted in vivo.

Place, publisher, year, edition, pages
2022. Vol. 14, no 4, article id 823
Keywords [en]
protein aggregation, secretion signal peptide, peptide engineering, drug design
National Category
Neurosciences Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-204559DOI: 10.3390/pharmaceutics14040823ISI: 000785290300001PubMedID: 35456657Scopus ID: 2-s2.0-85128454673OAI: oai:DiVA.org:su-204559DiVA, id: diva2:1657346
Available from: 2022-05-10 Created: 2022-05-10 Last updated: 2022-05-10Bibliographically approved

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Österlund, NicklasWärmländer, Sebastian K. T. S.Gräslund, Astrid

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