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

Nuria Mazo; Claudio D. Navo; Francesca Peccati; Jacopo Andreo; Cristina Airoldi; Gildas Goldsztejn; Pierre Çarçabal; Imanol Usabiaga; Mariona Sodupe; Stefan Wuttke; Jesús H. Busto; Jesús M. Peregrina; Emilio J. Cocinero; Gonzalo Jiménez-Osés

doi:10.1002/chem.202202913

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

Nuria Mazo, Claudio D. Navo, Francesca Peccati, Jacopo Andreo, Cristina Airoldi, Gildas Goldsztejn, Pierre Çarçabal, Imanol Usabiaga, Mariona Sodupe, Stefan Wuttke, Jesús H. Busto, Jesús M. Peregrina, Emilio J. Cocinero, Gonzalo Jiménez-Osés

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

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.

Original language	English
Article number	e202202913
Journal	Chemistry - A European Journal
Volume	29
Issue number	9
DOIs	https://doi.org/10.1002/chem.202202913
Publication status	Published - Feb 10 2023
Externally published	Yes

Keywords

hybrid peptides
sulfamidates
β-amino acids
β-amyloid
β-sheet breaker peptides

ASJC Scopus subject areas

Catalysis
Organic Chemistry

Access to Document

10.1002/chem.202202913

Cite this

Mazo, N., Navo, C. D., Peccati, F., Andreo, J., Airoldi, C., Goldsztejn, G., Çarçabal, P., Usabiaga, I., Sodupe, M., Wuttke, S., Busto, J. H., Peregrina, J. M., Cocinero, E. J., & Jiménez-Osés, G. (2023). Conformationally Restricted β-Sheet Breaker Peptides Incorporating Cyclic α-Methylisoserine Sulfamidates. Chemistry - A European Journal, 29(9), Article e202202913. https://doi.org/10.1002/chem.202202913

Mazo, N, Navo, CD, Peccati, F, Andreo, J, Airoldi, C, Goldsztejn, G, Çarçabal, P, Usabiaga, I, Sodupe, M, Wuttke, S, Busto, JH, Peregrina, JM, Cocinero, EJ & Jiménez-Osés, G 2023, 'Conformationally Restricted β-Sheet Breaker Peptides Incorporating Cyclic α-Methylisoserine Sulfamidates', Chemistry - A European Journal, vol. 29, no. 9, e202202913. https://doi.org/10.1002/chem.202202913

@article{cc5cee29a3e24da5abeeb8bb08c59c36,

title = "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.",

keywords = "hybrid peptides, sulfamidates, β-amino acids, β-amyloid, β-sheet breaker peptides",

author = "Nuria Mazo and Navo, {Claudio D.} and Francesca Peccati and Jacopo Andreo and Cristina Airoldi and Gildas Goldsztejn and Pierre {\c C}ar{\c c}abal and Imanol Usabiaga and Mariona Sodupe and Stefan Wuttke and Busto, {Jes{\'u}s H.} and Peregrina, {Jes{\'u}s M.} and Cocinero, {Emilio J.} and Gonzalo Jim{\'e}nez-Os{\'e}s",

note = "Publisher Copyright: {\textcopyright} 2022 Wiley-VCH GmbH.",

year = "2023",

month = feb,

day = "10",

doi = "10.1002/chem.202202913",

language = "English",

volume = "29",

journal = "Chemistry - A European Journal",

issn = "0947-6539",

publisher = "John Wiley and Sons Inc.",

number = "9",

}

TY - JOUR

T1 - Conformationally Restricted β-Sheet Breaker Peptides Incorporating Cyclic α-Methylisoserine Sulfamidates

AU - Mazo, Nuria

AU - Navo, Claudio D.

AU - Peccati, Francesca

AU - Andreo, Jacopo

AU - Airoldi, Cristina

AU - Goldsztejn, Gildas

AU - Çarçabal, Pierre

AU - Usabiaga, Imanol

AU - Sodupe, Mariona

AU - Wuttke, Stefan

AU - Busto, Jesús H.

AU - Peregrina, Jesús M.

AU - Cocinero, Emilio J.

AU - Jiménez-Osés, Gonzalo

PY - 2023/2/10

Y1 - 2023/2/10

N2 - 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.

AB - 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.

KW - hybrid peptides

KW - sulfamidates

KW - β-amino acids

KW - β-amyloid

KW - β-sheet breaker peptides

UR - http://www.scopus.com/inward/record.url?scp=85144845047&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85144845047&partnerID=8YFLogxK

U2 - 10.1002/chem.202202913

DO - 10.1002/chem.202202913

M3 - Article

C2 - 36377879

AN - SCOPUS:85144845047

SN - 0947-6539

VL - 29

JO - Chemistry - A European Journal

JF - Chemistry - A European Journal

IS - 9

M1 - e202202913

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this