Chiral amplification of oligopeptides in two-dimensional crystalline self-assemblies on water.
Differences in the two-dimensional packing arrangements of racemic and enantiomeric crystalline self-assemblies on the water surface of amphiphilic activated analogs of lysine and glutamic acid have been used to prepare oligopeptides of homochiral sequence and oligopeptides of single handedness from chiral nonracemic mixtures. The crystalline structures on the water surface were determined by grazing incidence x-ray diffraction and the diastereomeric composition of the oligopeptides by matrix-assisted laser desorption time-of-flight mass spectrometry with enantio-labeling. These results suggest that reactivity of ordered clusters at interfaces might have played a role in the generation of early homochiral biopolymers.
Zepik
Helmut
H
Department of Materials and Interfaces, Weizmann Institute of Science, 76100 Rehovot, Israel.
Shavit
Edna
E
Tang
Mao
M
Jensen
Torben R
TR
Kjaer
Kristian
K
Bolbach
Gérard
G
Leiserowitz
Leslie
L
Weissbuch
Isabelle
I
Lahav
Meir
M
D001704:Biopolymers; D003460:Crystallization; D018698:Glutamic Acid / Q000031:analogs & derivatives* / Q000737:chemistry; D008239:Lysine / Q000031:analogs & derivatives* / Q000737:chemistry; D009842:Oligopeptides / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013237:Stereoisomerism; D014867:Water; D014961:X-Ray Diffraction
D001704:Biopolymers; D009842:Oligopeptides; D014867:Water; D018698:Glutamic Acid; D008239:Lysine