BIOACTIVE PEPTIDES - X-RAY AND NMR CONFORMATIONAL STUDY OF [AIB(5, 6)-D-ALA(8)]CYCLOLINOPEPTIDE-A(492 views) DIBLASIO B, ROSSI F, BENEDETTI E, PAVONE V, SAVIANO M, PEDONE C, ZANOTTI G, TANCREDI T
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 1992 Oct 7; 114(21): 8277-8283.
Keywords: Cyclolinopeptide A, Cyclopeptide, Article, Drug Structure, Nuclear Magnetic Resonance,
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
Univ. di Napoli Federico II, Dipartimento di Chimica, Napoli, Italy
References: Not available.
BIOACTIVE PEPTIDES - X-RAY AND NMR CONFORMATIONAL STUDY OF [AIB(5, 6)-D-ALA(8)]CYCLOLINOPEPTIDE-A
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) angstrom, b = 19.85 (3) angstrom, c = 9.90 (1) angstrom, space group P2(1)2(1)2(1), Z = 4], shows the presence of five intramolecular N-H...O=C hydrogen bonds, with formation of one C17 ring structure, one alpha-turn (C-13), one gamma-turn (C7), and two beta-turns (C10, one of type III and one of type I). The Pro1-Pro2 peptide unit is cis (omega = 9-degrees), 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 - X-RAY AND NMR CONFORMATIONAL STUDY OF [AIB(5, 6)-D-ALA(8)]CYCLOLINOPEPTIDE-A
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