ISSN:
0006-3525
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
The peptide N-Boc-L-Pro-dehydro-Phe-L-Gly-OH was synthesized by the usual workup procedure and finally coupling the N-Boc-L-Pro-dehydro-Phe to glycine. The peptide crystallizes in monoclinic space group P21 with a = 8.951(4) Å, b = 5.677 (6) Å, c = 21.192(11) Å, β = 96.97(4)°, V = 1069(1) Å3, Z = 2, dm = 1.295(5) Mgm-3, and dc = 1.297(4) Mgm-3. The structure was determined by direct methods using SHELXS86. The structure was refined by the block-diagonal least-squares procedure to an R value of 0.074 for 1002 observed reflections. The C2α-C2β distance of 1.33(2) Å is an appropriate double bond length. The angle C2α-C2β-C2γ is 133(1)°. The peptide backbone torsion angles are θ1 = -167(1)°, ω0 = 179(1)°, φ1 = -48(1)°, ψ1 = 137(1)°, ω1 = 175(1)°, φ2 = 65(2)°, ψ2 = 15(2)°, ω2 = -179(1)°, and φ3 = -166(1)°. These values show that the Boc group has a trans-trans conformation while the peptide backbone adopts a β-turn II conformation, which is stablized by an intramolecular hydrogen bond of length of 3.05(1) Å. The structures of dehydro-Phe containing peptides suggest that the dehydro-Phe promotes the β-turn II conformation. The five-membered pyrrolidine ring of the Pro residue adopts an ideal Cγ-exo conformation with torsion angles χ11 = -24(1)°, χ12 = 34(1)°, χ13 = -30(1)°, χ14 = 15(1)°, and θ10 = 6(1)°. The side chain torsion angles in dehydro-Phe are χ21 = -1(2)°, χ22, 1 = -176(1)°, and χ22, 2 = 8(2)°. The Plane of C2α-C2β-C2γ is rotated with respect to the plane of the phenyl ring at 7(1)°, which indicates that the atoms of the side chain of dehydro-Phe are essentially coplanar. The molecules form a 21 screw axis related hydrogen-bonded rows along the b axis.
Additional Material:
3 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bip.360290306
Permalink
