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Conformationally Restricted β‐Sheet Breaker Peptides Incorporating Cyclic α‐Methylisoserine Sulfamidates

Abstract : Peptides containing variations of the β-amyloid hydrophobic core and five-membered sulfamidates derived from β-amino acid α-methylisoserine have been synthesized and fully characterized in the gas phase, solid state and in aqueous solution by a combination of experimental and computational techniques. The cyclic sulfamidate group effectively locks the secondary structure at the N-terminus of such hybrid peptides imposing a conformational restriction and stabilizing non-extended structures. This conformational bias, which is maintained in the gas phase, solid state and aqueous solution, is shown to be resistant to structure templating through assays of in vitro β-amyloid aggregation, acting as β-sheet breaker peptides with moderate activity.
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https://hal-cnrs.archives-ouvertes.fr/hal-03858954
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Submitted on : Friday, November 18, 2022 - 7:15:42 AM
Last modification on : Tuesday, December 6, 2022 - 4:06:21 AM

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Nuria Mazo, Claudio Navo, Francesca Peccati, Jacopo Andreo, Cristina Airoldi, et al.. Conformationally Restricted β‐Sheet Breaker Peptides Incorporating Cyclic α‐Methylisoserine Sulfamidates. Chemistry - A European Journal, In press, ⟨10.1002/chem.202202913⟩. ⟨hal-03858954⟩

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