ISSN:
0006-3525
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
In continuation of our studies on the structure and function of peptaibol antibiotics, the conformational properties of a sequence analogous to that of Trichodecenin I (Z-Gly-Gly-D-Leu-Aib-Gly-D-Ile-D-Leu-OMe, where Z = benzyloxycarbonyl, Aib = α-aminoisobutyric acid, and OMe = methyl ester) have been investigated crystallographically. This sequence is the mirror image of the naturally occurring molecule and also of the C-terminal heptapeptide of the related lipo-peptaibol Trichogin A IV (where, however, the Leu-OMe residue has replaced the original Leuol residue). The molecule crystallized in the monoclinic system, space group P21, Z = 4, and cell parameters a = 11.610(5), b = 33.342(8), c = 11.735(4) Å, β = 110.42(1)*, V = 4257(3) Å3. The crystallographic refinement converges at residual values of R = 0.047 and wR2 = 0.134 on F2. In the 1-5 segment the molecular conformation is virtually identical to that one reported from solution nmr studies of a similarly protected sequence [Biopolymers (1995), Vol. 35, pp. 21-29)] and is characterized by β-turns of type I at Gly1-Gly2, II′ at Leu3-Aib4, and I at Aib4-Gly5. In the crystal structure, a β-sheet-like arrangement is seen at the C-terminus. © 1996 John Wiley & Sons, Inc.
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
Permalink
