Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 109, Issue 39, Pages 15697-15701Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1210029109
Keywords
-
Categories
Funding
- National Science Foundation [NSF CHE-1011770]
- National Aeronautics and Space Administration Earth and Space Science Fellowship
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1011770] Funding Source: National Science Foundation
Ask authors/readers for more resources
We report unambiguous spectroscopic evidence of peptide bond formation at the air-water interface, yielding a possible mechanism providing insight into the formation of modern ribosomal peptide bonds, and a means for the emergence of peptides on early Earth. Protein synthesis in aqueous environments, facilitated by sequential amino acid condensation forming peptides, is a ubiquitous process in modern biology, and a fundamental reaction necessary in prebiotic chemistry. Such reactions, however, are condensation reactions, requiring the elimination of a water molecule for every peptide bond formed, and are thus unfavorable in aqueous environments both from a thermodynamic and kinetic point of view. We use the hydrophobic environment of the air-water interface as a favorable venue for peptide bond synthesis, and demonstrate the occurrence of this chemistry with in situ techniques using Langmuir-trough methods and infrared reflection absorption spectroscopy. Leucine ethyl ester (a small amino acid ester) first partitions to the water surface, then coordinates with Cu2+ ions at the interface, and subsequently undergoes a condensation reaction selectively forming peptide bonds at the air-water interface.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available