Bioactive peptides: conformational studies of [Tyr4] cyclolinopeptide(530 views) Saviano M, Rossi F, Filizola M, Isernia C, Di Blasio B, Benedetti E, Pedone C, Siemion IZ, Pedyczak A
Keywords: Cyclolinopeptide A, Cyclopeptide, Article, Protein Conformation, Drug Structure, Nuclear Magnetic Resonance, Conference Paper, Crystal Structure, Peptide Analysis, Stereochemistry, X Ray Diffraction, Amino Acid Sequence, Comparative Study, Crystallography, X-Ray, Hydrogen Bonding, Models, Molecular, Molecular Sequence Data, Protein Folding, Support, Non-U S Gov,
Affiliations: Istituto Chimica M.I.B. del C.N.R., Via Toiano 6, 80072 Arco Felice, Napoli, Italy
Ctro. di Studi Chim. del Farmaco, C.N.R., Roma, Italy
Univ.́ di Napoli Federico II, Dipartimento di Chimica, Napoli, Italy
CNR, Universita di Napoli Federico II, Dipartimento di Chimica, Italy.,
References: Not available.
Bioactive peptides: conformational studies of [Tyr4] cyclolinopeptide
The conformational analysis of [Aib5,6-D-Ala8]cyclolinopeptide A, in the solid state and solution, has been carried out by X-ray diffraction and NMR spectroscopy. The structure of the orthorhombic form, obtained from methanol-water mixture [a = 29.92 (3) Å, b = 19.85 (3) Å, c = 9.90 (1) Å, space group P212121 Z = 4], shows the presence of five intramolecular N-H⋯O=C hydrogen bonds, with formation of one C17 ring structure, one α-turn (C13), one γ-turn (C7), and two β-turns (C10, one of type III and one of type I). The Pro1-Pro2 peptide unit is cis (ω = 9°), all others are trans. The conformational study in solution by NMR spectroscopy indicates that, even at room temperature, the peptide is conformationally homogeneous; the structure determined is almost identical to that observed in the solid state. The solution study reveals, also, that the constraints imposed by the two Aib and D-Ala residues are particularly strong, because the NMR conformational parameters are only slightly affected by wide temperature variations and salt addition.
Bioactive peptides: conformational studies of [Tyr4] cyclolinopeptide
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