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Your search keyword '"peptidotriazolamers"' showing total 2 results
Start Over Descriptor "peptidotriazolamers" Topic alzheimer disease
2 results on '"peptidotriazolamers"'

1. Peptidotriazolamers Inhibit Aβ(1-42) Oligomerization and Cross a Blood-Brain-Barrier Model.

Author

Tonali N, Hericks L, Schröder DC, Kracker O, Krzemieniecki R, Kaffy J, Le Joncour V, Laakkonen P, Marion A, Ongeri S, Dodero VI, and Sewald N

Subjects
Amides metabolism, Amyloid beta-Peptides metabolism, Cell Survival, Humans, Models, Biological, Models, Molecular, Molecular Conformation, Molecular Structure, Peptide Fragments metabolism, Protein Binding, Structure-Activity Relationship, Triazoles metabolism, Alzheimer Disease metabolism, Amyloid beta-Peptides chemistry, Blood-Brain Barrier metabolism, Peptide Fragments chemistry, Peptides chemistry, Protein Aggregates drug effects, Triazoles chemistry
Abstract

In peptidotriazolamers every second peptide bond is replaced by a 1H-1,2,3-triazole. Such foldamers are expected to bridge the gap in molecular weight between small-molecule drugs and protein-based drugs. Amyloid β (Aβ) aggregates play an important role in Alzheimer's disease. We studied the impact of amide bond replacements by 1,4-disubstituted 1H-1,2,3-triazoles on the inhibitory activity of the aggregation "hot spots" K 16 LVFF 20 and G 39 VVIA 42 in Aβ(1-42). We found that peptidotriazolamers act as modulators of the Aβ(1-42) oligomerization. Some peptidotriazolamers are able to interfere with the formation of toxic early Aβ oligomers, depending on the position of the triazoles, which is also supported by computational studies. Preliminary in vitro results demonstrate that a highly active peptidotriazolamer is also able to cross the blood-brain-barrier., (© 2021 The Authors. ChemPlusChem published by Wiley-VCH GmbH.)

Published
2021
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2. Peptidotriazolamers Inhibit Aβ(1–42) Oligomerization and Cross a Blood‐Brain‐Barrier Model

Author

Nicolo Tonali, Julia Kaffy, Vadim Le Joncour, David C. Schröder, Pirjo Laakkonen, Loreen Hericks, Antoine Marion, Norbert Sewald, Verónica I. Dodero, Sandrine Ongeri, Oliver Kracker, Radosław Krzemieniecki, CAN-PRO - Translational Cancer Medicine Program, Research Programs Unit, University of Helsinki, and Pirjo Maarit Laakkonen / Principal Investigator

Subjects
Models, Molecular, Amyloid β, BETA-HAIRPIN MIMICS, Cell Survival, Peptidomimetic, Molecular Conformation, 010402 general chemistry, Blood–brain barrier, Inhibitory postsynaptic potential, Models, Biological, 01 natural sciences, PROTEIN-PROTEIN INTERACTIONS, FOLDAMERS, Protein Aggregates, Structure-Activity Relationship, Alzheimer Disease, mental disorders, oligomerization inhibitors, medicine, Humans, Peptide bond, amyloids, &#945, Amyloid beta-Peptides, &#946, Molecular Structure, 010405 organic chemistry, Chemistry, Aβ oligomers, General Chemistry, AGGREGATION, Triazoles, Amides, Peptide Fragments, In vitro, 0104 chemical sciences, 3. Good health, MODULATE, medicine.anatomical_structure, Blood-Brain Barrier, peptidomimetics, Biophysics, 3111 Biomedicine, peptidotriazolamers, Peptides, Protein Binding
Abstract

In peptidotriazolamers every second peptide bond is replaced by a 1H-1,2,3-triazole. Such foldamers are expected to bridge the gap in molecular weight between small-molecule drugs and protein-based drugs. Amyloid beta (Abeta) aggregates play an important role in Alzheimer's disease. We studied the impact of amide bond replacements by 1,4-disubstituted 1H-1,2,3-triazoles on the inhibitory activity of the aggregation "hot spots" K16 LVFF20 and G39 VVIA42 in Abeta(1-42). We found that peptidotriazolamers act as modulators of the Abeta(1-42) oligomerization. Some peptidotriazolamers are able to interfere with the formation of toxic early Abeta oligomers, depending on the position of the triazoles, which is also supported by computational studies. Preliminary in vitro results demonstrate that a highly active peptidotriazolamer is also able to cross the blood-brain-barrier. © 2021 The Authors. ChemPlusChem published by Wiley-VCH GmbH.

Published
2021

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