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...

Full description

Saved in:
Bibliographic Details
Published inScience (American Association for the Advancement of Science) Vol. 295; no. 5558; pp. 1266 - 1269
Main Authors Zepik, Helmut, Shavit, Edna, Tang, Mao, Jensen, Torben R., Kjaer, Kristian, Bolbach, Gérard, Leiserowitz, Leslie, Weissbuch, Isabelle, Lahav, Meir
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for the Advancement of Science 15.02.2002
American Association for the Advancement of Science
The American Association for the Advancement of Science
Subjects
Biological and medical sciences
Biopolymers
Chirality
Crystallites
Crystallization
Crystallography
Enantiomers
Fundamental and applied biological sciences. Psychology
Glutamic Acid - analogs & derivatives
Glutamic Acid - chemistry
Handedness
Lysine - analogs & derivatives
Lysine - chemistry
Molecular and cellular biology
Molecules
Monomers
Oligopeptides
Oligopeptides - chemistry
Organic Chemistry
Peptides
Polymerization
Self assembly
Solid solutions
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Spectrum analysis
Statistical distributions
Stereoisomerism
Water
X-Ray Diffraction
United States
Online AccessGet full text

Cover

More Information
Summary: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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1065625