Researchers with the Macromolecules and Interfaces Institute (MII www.mii.vt.edu) at Virginia Tech report such a development in the online issue for the Journal of the American Chemical Society, in the article, "Aggregation of Rod-Coil Block Copolymers Containing Rigid Polyampholyte Blocks in Aqueous Solution" (10.1021/ja070422+) and at the 233rd National Meeting of the American Chemical Society (ACS) in Chicago, March 25-29.
S. Richard Turner, MII director and research professor of chemistry at Virginia Tech, and Min Mao, a Ph.D. candidate in polymer chemistry, report the synthesis of a new family of charged, rod-like block copolymers. Only as long as a fraction of the diameter of human hair, the tiny rods can be either positive or negative, or can have alternating positive and negative charges along the backbone. The rods self-assemble and the aggregated structures are remarkable stable in saline solution, Turner said.
"The early results of this study suggest that these charged polymers self-assemble by like-charge interactions similar to such natural polymers as DNA," said Turner. "The stable self-assembled structures could have potential applications in drug delivery and gene delivery systems."
But more immediate, "These unique block copolymers can be instructive models in understanding the forces that lead to the dense packing of DNA when complexed with viruses and other polymers," he said.
Susan Trulove | EurekAlert!
Climate Impact Research in Hannover: Small Plants against Large Waves
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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