The 1,3‐diyne linker as a rigid “ i , i +7” staple for α‐helix stabilization: Stereochemistry at work | Zendy

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

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The 1,3‐diyne linker as a rigid “ i , i +7” staple for α‐helix stabilization: Stereochemistry at work

Author(s) -

Verlinden Steven,

Geudens Niels,

Van holsbeeck Kevin,

Mannes Morgane,

Martins José C.,

Verniest Guido,

Ballet Steven

Publication year - 2019

Publication title -

journal of peptide science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.475

H-Index - 66

eISSN - 1099-1387

pISSN - 1075-2617

DOI - 10.1002/psc.3194

Subject(s) - linker , chemistry , stereochemistry , peptide , helix (gastropod) , crystallography , biochemistry , biology , computer science , ecology , snail , operating system

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.

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