Incorporation of Ahc into Model Dipeptides as an Inducer of a Beta-Turn with a Distorted Amide Bond. Conformational Analysis

  1. Avenoza, A. 1
  2. Busto, J.H. 1
  3. Peregrina, J.M. 1
  4. Rodríguez, F. 1
  1. 1 Universidad de La Rioja
    info

    Universidad de La Rioja

    Logroño, España

    ROR https://ror.org/0553yr311

Aldizkaria:
Journal of Organic Chemistry

ISSN: 0022-3263

Argitalpen urtea: 2002

Alea: 67

Zenbakia: 12

Orrialdeak: 4241-4249

Mota: Artikulua

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DOI: 10.1021/JO016406R PMID: 12054960 SCOPUS: 2-s2.0-0037077017 WoS: WOS:000176173700032 GOOGLE SCHOLAR

Beste argitalpen batzuk: Journal of Organic Chemistry

Gordailu instituzionala: lock_openSarbide irekia Editor

Garapen Iraunkorreko Helburuak

Laburpena

The proline residue of dipeptides Ser-Pro and Pro-Ser has been replaced by 7-azabicyclo[2.2.1]heptane-1-carboxylic acid (Ahc), a conformationally restricted analogue of proline that is capable of mimicking distorted amides. The conformational analysis of the new peptides in the solid state revealed that the Ahc-Ser sequence displays a type I β-turn, which includes a distorted amide bond. In contrast, the Ser-Ahc sequence exists in a nonfolded structure.