The 1,3-diyne linker as a rigid "i,i+7" staple for alpha-helix stabilization: Stereochemistry at work. IF 1.877

Steven Verlinden; Niels Geudens; Kevin Van holsbeeck; Morgane Mannes; Jose C. Martins; Guido Verniest; Steven Ballet

doi:10.1002/psc.3194

The 1,3-diyne linker as a rigid "i,i+7" staple for alpha-helix stabilization: Stereochemistry at work. IF 1.877

Steven Verlinden, Niels Geudens, Kevin Van holsbeeck, Morgane Mannes, Jose C. Martins, Guido Verniest, Steven Ballet

Onderzoeksoutput: Article › peer review

4 Citaten (Scopus)

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Short alphahelical peptide sequences were stabilized through Glaser-Hay couplings of propargylated l- and/or d-serine residues at positions i and i+7. NMR analysis confirmed a full stabilization of the helical structure when a d-Ser (i), l-Ser (i+7) combination was applied. In case two l-Ser residues were involved in the cyclization, the helical conformation is disrupted outside the peptide's macrocycle.

Originele taal-2	English
Aantal pagina's	9
Tijdschrift	Journal of Peptide Science
Volume	25
Nummer van het tijdschrift	7
DOI's	https://doi.org/10.1002/psc.3194
Status	Published - jul. 2019

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title = "The 1,3-diyne linker as a rigid {"}i,i+7{"} staple for alpha-helix stabilization: Stereochemistry at work. IF 1.877",

abstract = "Short alphahelical peptide sequences were stabilized through Glaser-Hay couplings of propargylated l- and/or d-serine residues at positions i and i+7. NMR analysis confirmed a full stabilization of the helical structure when a d-Ser (i), l-Ser (i+7) combination was applied. In case two l-Ser residues were involved in the cyclization, the helical conformation is disrupted outside the peptide's macrocycle.",

keywords = "constrained peptides, Glaser-Hay coupling, helix stabilization, peptide stapling",

author = "Steven Verlinden and Niels Geudens and {Van holsbeeck}, Kevin and Morgane Mannes and Martins, {Jose C.} and Guido Verniest and Steven Ballet",

year = "2019",

month = jul,

doi = "10.1002/psc.3194",

language = "English",

volume = "25",

journal = "Journal of Peptide Science",

issn = "1075-2617",

publisher = "John Wiley and Sons Ltd",

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T1 - The 1,3-diyne linker as a rigid "i,i+7" staple for alpha-helix stabilization: Stereochemistry at work. IF 1.877

AU - Verlinden, Steven

AU - Geudens, Niels

AU - Van holsbeeck, Kevin

AU - Mannes, Morgane

AU - Martins, Jose C.

AU - Verniest, Guido

AU - Ballet, Steven

PY - 2019/7

Y1 - 2019/7

N2 - Short alphahelical peptide sequences were stabilized through Glaser-Hay couplings of propargylated l- and/or d-serine residues at positions i and i+7. NMR analysis confirmed a full stabilization of the helical structure when a d-Ser (i), l-Ser (i+7) combination was applied. In case two l-Ser residues were involved in the cyclization, the helical conformation is disrupted outside the peptide's macrocycle.

AB - Short alphahelical peptide sequences were stabilized through Glaser-Hay couplings of propargylated l- and/or d-serine residues at positions i and i+7. NMR analysis confirmed a full stabilization of the helical structure when a d-Ser (i), l-Ser (i+7) combination was applied. In case two l-Ser residues were involved in the cyclization, the helical conformation is disrupted outside the peptide's macrocycle.

KW - constrained peptides

KW - Glaser-Hay coupling

KW - helix stabilization

KW - peptide stapling

UR - http://www.scopus.com/inward/record.url?scp=85067473185&partnerID=8YFLogxK

U2 - 10.1002/psc.3194

DO - 10.1002/psc.3194

M3 - Article

SN - 1075-2617

VL - 25

JO - Journal of Peptide Science

JF - Journal of Peptide Science

IS - 7

ER -

The 1,3-diyne linker as a rigid "i,i+7" staple for alpha-helix stabilization: Stereochemistry at work. IF 1.877

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