Unusual conformational preferences of β-alanine containing cyclic peptides. VII(138 visite) Lombardi A, Saviano M, Nastri F, Maglio O, Mazzeo M, Pedone C, Isernia C, Pavone V
Parole chiave: Conformations, Hydrogen Bonds, Molecular Structure, Single Crystals, Synthesis (chemical), X Ray Analysis, Conformational Preferences, Cyclic Peptides, Intramolecular Hydrogen Bond, Proteins, Beta Alanine, Cyclopeptide, Pentapeptide, Article, Peptide Synthesis, Protein Conformation, X Ray Crystallography, Amino Acid Sequence, Beta-Alanine, Molecular Sequence Data,
Affiliazioni:
CNR and CEINGE, Centro Interdipartimentale, University of Naples Federico II, via Mezzocannone 4, 80134 Napoli, Italy
Riferimenti:
Non disponibile.
In the present paper we describe the synthesis, purification, and single crystal x-ray analysis of the cyclic pentapeptide cyclo-(Pro-Phe-Phe-β-Ala- β-Ala). This compound crystallizes in the orthorhombic space group P212121 from methanol and adopts in the solid state an unusual conformation characterized by a cis β-Ala5-Pro1 peptide bond and by an intramolecular hydrogen bond stabilizing a C11- and a C12-ring structure. The C11 structure contains the Phe3 and the β-Ala4 at the corner position of the turn; it is the first observation of a type II β-turn enlargement due to the insertion of an extra methylene group of the β- alanine residue. The rest of the molecule participates in a newly characterized C12-ring structure, which incorporates a β-Ala residue at position i of the turn.
191 Records (189 escludendo Abstract e Conferenze). Impact factor totale: 751.868 (746.33 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 805.679 (799.964 escludendo Abstract e Conferenze).
ibb.cnr.it