Jan 5, 2011 11:40 GMT  ·  By
Simple peptides access both the physical properties and the long-range molecular order that is critical to the origins of chemical evolution
   Simple peptides access both the physical properties and the long-range molecular order that is critical to the origins of chemical evolution

For many years, researchers, scientists and philosophers have been proposing that the origin of life can be found in various types of arrangements made up of four basic elements – earth, water, air and fire. A new finding now shows a possible avenue that may have linked inorganic to organic chemistry.

In a groundbreaking discovery, experts were able to show that molecules called peptides are capable of self-arranging into by-layer membranes, similar to the structures that surround cells.

It could be that these molecules are the missing link experts have been looking for, connecting the inventory of chemicals available on Earth before the first lifeforms appeared to the neatly-organized scaffolding that currently supports most living things.

“This is a boon to our understanding of large, structural assemblies of molecules,” explains the co-leader of the research effort, expert David Lynn, the Chemistry Chair at the Emory University.

Experts from Emory's departments of chemistry, biology and physics were also involved in the study. “We’ve proved that peptides can organize as bi-layers, and we’ve generated the first, real-time imaging of the self-assembly process,” Lynn adds.

“We can actually watch in real-time as these nano-machines make themselves,” he goes on to say, adding that one of the most fundamental traits of biology is that it can organize things and structured within compartments and along surfaces.

This ability spawns the cell membrane's bi-layer phospholipids, the double-helix structure of DNA, as well as the formation of other arrays that self-assemble to underly the general architecture of life.

“We’ve shown that peptides can form the kind of membranes needed to create long-range order,” explains Seth Childers, a chemistry graduate student at Emory University.

“What’s also interesting is that these peptide membranes may have the potential to function in a complex way, like a protein,” adds the expert, who was the lead author of the new paper.

The work was published recently in an issue of the German Chemical Society’s respected journal, Angewandte Chemie, Daily Galaxy reports. The data will also appear in an issue of the Journal of the American Chemical Society.

“In order to form nuclei, which become the templates for growth, the peptides first repel water. Once the peptides form the template, we can now see how they assemble from the outer edges,” says Emory chemistry graduate student and post-doctoral fellow in neuroscience Yan Liang.

The results of the investigation could also be used to underlie the creation of new cures and treatments for conditions such as Alzheimer’s disease and Type II diabetes, among others.