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• W4283716962 abstract "The cyclin-dependent kinase (CDK5) forms a stable complex with its activator p25, leading to the hyperphosphorylation of tau proteins and to the formation of plaques and tangles that are considered to be one of the typical causes of Alzheimer’s disease (AD). Hence, the pathological CDK5–p25 complex is a promising therapeutic target for AD. Small peptides, obtained from the truncation of CDK5 physiological activator p35, have shown promise in inhibiting the pathological complex effectively while also crossing the blood–brain barrier. One such small 24-residue peptide, p5, has shown selective inhibition toward the pathological complex in vivo. Our previous research focused on the characterization of a computationally predicted CDK5–p5 binding mode and of its pharmacophore, which was consistent with competitive inhibition. In continuation of our previous work, herein, we investigate four additional binding modes to explore other possible mechanisms of interaction between CDK5 and p5. The quantitative description of the pharmacophore is consistent with both competitive and allosteric p5-induced inhibition mechanisms of CDK5–p25 pathology. The gained insights can direct further in vivo/in vitro tests and help design small peptides, linear or cyclic, or peptidomimetic compounds as adjuvants of orthosteric inhibitors or as part of a cocktail of drugs with enhanced effectiveness and lower side effects." @default.
• W4283716962 created "2022-07-01" @default.
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• W4283716962 date "2022-06-30" @default.
• W4283716962 modified "2023-09-25" @default.
• W4283716962 title "Computational Study of the Allosteric Effects of p5 on CDK5–p25 Hyperactivity as Alternative Inhibitory Mechanisms in Neurodegeneration" @default.
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• W4283716962 doi "https://doi.org/10.1021/acs.jpcb.2c02868" @default.
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• W4283716962 hasPublicationYear "2022" @default.
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