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Protein mimetic amyloid inhibitor potently abrogates cancer-associated mutant p53 aggregation and restores tumor suppressor function

Amyloid aggregation of mutant p53 contributes to its loss of tumor suppressor function and oncogenic gain-of-function. Here, the authors use a protein mimetic to abrogate mutant p53 aggregation and rescue p53 function, which inhibits cancer cell proliferation in vitro and halts tumor growth in vivo.

L. Palanikumar
Laura Karpauskaite
Mazin Magzoub
ResearchOpen Access25 Jun 2021
Nature Communications

Volume: 12, P: 1-24
Protein mimetic 2D FAST rescues alpha synuclein aggregation mediated early and post disease Parkinson’s phenotypes

The aggregation of the neuronal protein α-Synuclein is associated with the onset of Parkinson’s disease. Here the authors report a two-dimensional Fragment Assisted Structure-based technique to find antagonists of α-Synuclein aggregation and show its promise for identifying lead therapeutics for Parkinson’s disease.

Nicholas H. Stillman
Johnson A. Joseph
Sunil Kumar
ResearchOpen Access30 Apr 2024
Nature Communications

Volume: 15, P: 1-25
Foldamers reveal and validate therapeutic targets associated with toxic α-synuclein self-assembly

Inhibiting alpha-synuclein self-assembly into amyloid structures, associated with Parkinson’s disease, is a potential therapeutic intervention. Here, the authors identify the domains/sequences that are essential for alpha-synuclein aggregation and test the activity of foldamer-based antagonists to identify potential therapeutic targets.

Jemil Ahmed
Tessa C. Fitch
Sunil Kumar
ResearchOpen Access27 Apr 2022
Nature Communications

Volume: 13, P: 1-17

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Protein mimetic amyloid inhibitor potently abrogates cancer-associated mutant p53 aggregation and restores tumor suppressor function

Protein mimetic 2D FAST rescues alpha synuclein aggregation mediated early and post disease Parkinson’s phenotypes

Foldamers reveal and validate therapeutic targets associated with toxic α-synuclein self-assembly

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