Highly potent peptide therapeutics to prevent protein aggregation in huntington’s disease

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buir.contributor.authorKhan, Anooshay
buir.contributor.authorÖzçelik, Cemile Elif
buir.contributor.authorBegli, Özge
buir.contributor.authorOğuz, Oğuzhan
buir.contributor.authorKasırga, Talip Serkan
buir.contributor.authorŞeker, Urartu Özgür Şafak
buir.contributor.orcidKhan, Anooshay|0000-0002-1577-2279
buir.contributor.orcidOğuz, Oğuzhan|0000-0003-3128-7334
buir.contributor.orcidKasırga, Talip Serkan|0000-0003-3510-5059
buir.contributor.orcidŞeker, Urartu Özgür Şafak|0000-0002-5272-1876
dc.citation.epage1826en_US
dc.citation.issueNumber12
dc.citation.spage1821
dc.citation.volumeNumber14
dc.contributor.authorKhan, Anooshay
dc.contributor.authorÖzçelik, Cemile Elif
dc.contributor.authorBegli, Özge
dc.contributor.authorOğuz, Oğuzhan
dc.contributor.authorKesici, M. S.
dc.contributor.authorKasırga, Talip Serkan
dc.contributor.authorÖzçubukcu, S.
dc.contributor.authorYuca, E.
dc.contributor.authorŞeker, Urartu Özgür Şafak
dc.date.accessioned2024-03-11T11:08:26Z
dc.date.available2024-03-11T11:08:26Z
dc.date.issued2023-12-14
dc.departmentInstitute of Materials Science and Nanotechnology (UNAM)
dc.departmentAysel Sabuncu Brain Research Center (BAM)
dc.description.abstractHuntington’s disease (HD) is a neurodegenerative disorder resulting from a significant amplification of CAG repeats in exon 1 of the Huntingtin (Htt) gene. More than 36 CAG repeats result in the formation of a mutant Htt (mHtt) protein. These amino-terminal mHtt fragments lead to the formation of misfolded proteins, which then form aggregates in the relevant brain regions. Therapies that can delay the progression of the disease are imperative to halting the course of the disease. Peptide-based drug therapies provide such a platform. Inhibitory peptides were screened against monomeric units of both wild type (Htt(Q25)) and mHtt fragments, Htt(Q46) and Htt(Q103). Fibril kinetics was studied by utilizing the Thioflavin T (ThT) assay. Atomic force microscopy was also used to study the influence of the peptides on fibril formation. These experiments demonstrate that the chosen peptides suppress the formation of fibrils in mHtt proteins and can provide a therapeutic lead for further optimization and development.
dc.description.provenanceMade available in DSpace on 2024-03-11T11:08:26Z (GMT). No. of bitstreams: 1 Highly_potent_peptide_therapeutics_to_prevent_protein_aggregation_in_huntington’s_disease.pdf: 4556702 bytes, checksum: 10856cde3d20c7b88a571b6460bae3c2 (MD5) Previous issue date: 2023-12-14en
dc.identifier.doi10.1021/acsmedchemlett.3c00415
dc.identifier.issn19485875
dc.identifier.urihttps://hdl.handle.net/11693/114503
dc.language.isoen
dc.publisherAmerican Chemical Society
dc.relation.isversionofhttps://dx.doi.org/10.1021/acsmedchemlett.3c00415
dc.source.titleACS Medicinal Chemistry Letters
dc.subjectHuntington’s disease
dc.subjectPeptide-based drug therapy
dc.subjectHuntingtin
dc.subjectHtt aggregation
dc.subjectInhibition
dc.titleHighly potent peptide therapeutics to prevent protein aggregation in huntington’s disease
dc.typeArticle

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