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α-Alkylation of Ketones via Enolate Ions01:10

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Ketones with α protons are deprotonated by strong bases like lithium diisopropylamide (LDA) to form enolate ions. The anion is stabilized by resonance, and its hybrid structure exhibits negative charges on the carbonyl oxygen and the α carbon. This ambident nucleophile can attack an electrophile via two possible sites: the carbonyl oxygen, known as O-attack, or the α carbon, known as C-attack. The nucleophilic attack via the carbanionic site is preferred. This is due to the...
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α-Alkylation of ketones is achieved in the presence of alkyl halides and a base. The reaction proceeds via the formation of an enolate ion followed by nucleophilic substitution. The choice of base employed is essential as it is the key factor in determining the reaction outcome.
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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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By replacing an α-hydrogen with a halogen, acid-catalyzed α-halogenation of aldehydes or ketones yields a monohalogenated product
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α-Halogenation of aldehydes and ketones is a reaction involving the substitution of α hydrogens with halogens in the presence of a base.  The reaction begins with the abstraction of  α hydrogen by the base to produce a nucleophilic enolate ion. This intermediate undergoes a subsequent nucleophilic substitution with the halogen to produce a monohalogenated carbonyl compound. If the starting substrate has more than one α hydrogen, it is difficult to stop the reaction...
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Peptidomimetics Inspired by α-Synuclein or Its Chaperone αB-Crystallin Differentially Modulate α-Synuclein

Nicolo Bisi1, Josine Kothuis2, Julia Kaffy1

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Journal of Medicinal Chemistry
|January 23, 2026
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Summary

Researchers developed small peptidomimetics that interfere with alpha-Synuclein (αSyn) aggregation, a key factor in Parkinson's disease. This breakthrough offers potential new therapeutic strategies for synucleinopathies and other amyloid diseases.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Drug Discovery

Background:

  • Alpha-Synuclein (αSyn) protein aggregation in neurons causes synucleinopathies like Parkinson's disease.
  • Pathological αSyn forms toxic oligomers and fibrils, leading to neuronal death.
  • Currently, no treatments exist to prevent fatal synucleinopathies.

Purpose of the Study:

  • To design and evaluate small peptidomimetics that inhibit αSyn aggregation.
  • To explore the relationship between peptidomimetic structure, sequence, and their effect on αSyn aggregation.
  • To develop novel therapeutic strategies for neurodegenerative diseases characterized by protein aggregation.

Main Methods:

  • Designed peptidomimetics inspired by αSyn aggregates and the chaperone protein αB-Crystallin.
  • Utilized in vitro and cellular assays to assess the compounds' impact on αSyn aggregation.
  • Investigated the correlation between peptidomimetic characteristics and their anti-aggregation activity.

Main Results:

  • One αB-Crystallin-based peptidomimetic effectively interfered with αSyn folding and aggregation.
  • The compound reduced the formation of toxic αSyn oligomers.
  • The study demonstrated the promotion of off-pathway aggregation by the peptidomimetic.

Conclusions:

  • Physiological chaperone proteins can be mimicked by small peptide derivatives.
  • This approach provides a new strategy for designing inhibitors of amyloid protein aggregation.
  • The findings pave the way for potential treatments for neurodegenerative and systemic amyloid diseases.