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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Aggregation Limiting Cell-Penetrating Peptides Derived from Protein Signal Sequences.

Ly Porosk1, Heleri Heike Härk1, Renata Naporano Bicev2

  • 1Institute of Technology, University of Tartu, Nooruse 1, 50411 Tartu, Estonia.

International Journal of Molecular Sciences
|March 11, 2023
PubMed
Summary
This summary is machine-generated.

New peptides derived from transthyretin show promise in reducing amyloid-beta aggregation, a key feature of Alzheimer's disease (AD). These modified peptides also exhibit potential anti-inflammatory effects and cell-penetrating properties for AD therapy.

Keywords:
Alzheimer’s diseaseaggregationamyloid betacell-penetrating peptidespeptides

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Area of Science:

  • Neurodegenerative diseases
  • Biochemistry
  • Molecular biology

Background:

  • Alzheimer's disease (AD) is a leading cause of dementia, characterized by amyloid-beta (Aβ) plaques and neurofibrillary tangles.
  • Current treatments for AD are limited, highlighting the need for novel therapeutic strategies targeting disease mechanisms.
  • Understanding the heterogeneous pathophysiology of AD is crucial for developing effective interventions.

Purpose of the Study:

  • To investigate novel peptide sequences for their ability to reduce amyloid-beta (Aβ) aggregation in vitro.
  • To explore the potential of modified signal peptides, including those derived from transthyretin, as therapeutic agents for Alzheimer's disease.
  • To assess the cell-penetrating and anti-inflammatory properties of these novel peptides.

Main Methods:

  • In vitro assessment of amyloid-beta (Aβ) aggregation using modified signal peptides, including transthyretin-derived sequences.
  • Evaluation of cell-penetrating peptide (CPP) properties of modified peptides in mammalian cells.
  • Utilizing an Aβ-EGFP fusion protein to efficiently monitor aggregation reduction and CPP efficacy.

Main Results:

  • Transthyretin-derived peptides, similar to NCAM1 signal sequences, effectively reduce amyloid-beta (Aβ) aggregation in vitro.
  • Modified signal peptides demonstrated cell-penetrating properties and are predicted to possess anti-inflammatory effects.
  • The Aβ-EGFP fusion protein system proved effective for assessing peptide-mediated aggregation reduction and CPP activity.

Conclusions:

  • Novel modified signal peptides, particularly those derived from transthyretin, represent a promising therapeutic avenue for reducing amyloid-beta (Aβ) aggregation in Alzheimer's disease (AD).
  • These peptides offer potential dual benefits of targeting Aβ aggregation and exhibiting anti-inflammatory properties.
  • The developed Aβ-EGFP fusion protein assay provides a robust platform for future screening of AD-targeting peptides.