Alpha-hydroxymethylserine as a peptide building block: synthetic and structural aspects.
A synthetic methodology has been developed for peptide bond formation with alpha-hydroxmethylserine as the carboxyl or amino component and also for the preparation of homo-sequences. The key intermediate, O,O-protected alpha-hydroxymethylserine in the form of an isopropylidene derivative, is easily accessible and represents the first example of a heterocyclic C(alpha,alpha)-disubstituted amino acid containing an 1,3-dioxane ring. The use of this intermediate facilitates protection of the sterically hindered amino and carboxyl groups and is advantageous for the coupling and deprotection steps. X-ray structure determination of Z-HmS(Ipr)-Ala-OMe revealed that the two crystallographically independent molecules present in the asymmetric unit adopt an S-shaped conformation. In the one molecule the achiral HmS(Ipr) residue has the torsion angle values (phi = 61.4 degrees, psi, = 40.8 degrees) in the left-handed helical region of the Ramachandran map, while in the second molecule the negative torsion angles (phi = -60.1 degrees, psi = -44.4 degrees) are associated with the right-handed helix.
Stasiak
M
M
Institute of Organic Chemistry, Technical University, Lódź, Poland.
Wolf
W M
WM
Leplawy
M T
MT
D002851:Chromatography, High Pressure Liquid; D018360:Crystallography, X-Ray; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D012694:Serine / Q000031:analogs & derivatives* / Q000737:chemistry; D016339:Spectrometry, Mass, Fast Atom Bombardment
D012694:Serine