Monoclinic polymorph of Boc‐Trp‐Ile‐Ala‐Aib‐Ile‐Val‐Aib‐Leu‐Aib‐Pro‐OMe(anhydrous)

Abstract
The structures of two crystal forms of Boc-Trp-Ile-Ala-Aib-Ile-Val-Aib-Leu-Aib-Pro-OMe have been determined. The triclinic form (P1, Z = 1) from DMSO/H2O crystallizes as a dihydrate (Karle, Sukumar and Balaram (1986) Proc. Natl. Acad. Sci. USA 83, 9284-9288). The monoclinic form (P21, Z = 2) crystallized from dioxane is anhydrous. The conformation of the peptide is essentially the same in both crystal systems, but small changes in conformational angles are associated with a shift of the helix from a predominantly .alpha.-type to a predominantly 310-type. The r.m.s. deviation of 33 atoms in the backbone and C.beta. positions of residues 2-8 is only 0.29 .ANG. between molecules in the two polymorphs. In both space groups, the helical molecules pack in a parallel fashion, rather than antiparallel. The only intermolecular hydrogen bonding is head-to-tail between helices. There are no lateral hydrogen bonds. In the P21 cell, a = 9.422(2).ANG., b = 36.392(11).ANG., c = 10.548(2).ANG., .beta. = 111.31(2).degree. and V = 3369.3.ANG.3 for 2 molecules of C60H97N11O13 per cell.

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