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UO-Berkeley Lab unveil new nano-sized synthetic scaffolding technique
Date:9/2/2014

standing of the peptoid assembly mechanism should enable us to scale-up to produce large quantities, or scale- down, using microfluidics, to screen many different nanosheets for novel functions."

Zuckermann and Richmond are the corresponding authors on the paper. Additional co-authors are Menglu Qian and Caroline Proulx, both of LBNL.

Like natural proteins, synthetic proteins fold and conform into structures that allow them to do specific functions. In his earlier work, Zuckermann's team at LBNL's Molecular Foundry discovered a technique to synthesize peptoids into sheets that were just a few nanometers thick but up to 100 micrometers in length. These were among the largest and thinnest free-floating organic crystals ever made, with an area-to-thickness equivalent of a plastic sheet covering a football field.

"Peptoid nanosheet properties can be tailored with great precision," Zuckermann says, "and since peptoids are less vulnerable to chemical or metabolic breakdown than proteins, they are a highly promising platform for self-assembling bio-inspired nanomaterials."

To create the new version of the nanosheets, the research team used vibrational sum frequency spectroscopy to probe the molecular interactions between the peptoids as they assemble at the oil-water interface. The work showed that peptoid polymers adsorbed to the interface are highly ordered in a way that is influenced by interactions between neighboring molecules.

The substitution of oil in place of air creates a raft of new opportunities for the engineering and production of peptoid nanosheets, the researchers said. The oil phase, for example, could contain chemical reagents, serve to minimize evaporation of the aqueous phase or enable microfluidic production.


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Contact: Jim Barlow
jebarlow@uoregon.edu
541-346-3481
University of Oregon
Source:Eurekalert

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