Syndicate content

Archive - May 1, 2018

Date
  • All
  • 1
  • 2
  • 3
  • 4
  • 5
  • 6
  • 7
  • 8
  • 9
  • 10
  • 11
  • 12
  • 13
  • 14
  • 15
  • 16
  • 17
  • 18
  • 19
  • 20
  • 21
  • 22
  • 23
  • 24
  • 25
  • 26
  • 27
  • 28
  • 29
  • 30
  • 31

Designer Peptoids Mimic Surfactant Proteins & Reduce Surface Tension in the Lungs, Restoring Breathing Capacity in Injured Lungs in Rat Model—Results “Open Up New Frontiers”

A Stanford University researcher has bioengineered an effective protein mimic that restored breathing capacity to the injured lungs of rats, according to a new study. This synthetic product could lead to better, cheaper treatments for acute lung injury in humans. When used in the rats, it equaled or outperformed a costly animal-derived counterpart in several physiological measures, the study said. A paper describing the research was published online May 1 in Scientific Reports. The open-access article is titled “Effective in vivo treatment of acute lung injury with helical, amphipathic peptoid mimics of pulmonary surfactant proteins. Imagine the force you'd need to blow up a balloon whose surface area nearly matched that of a tennis court. Imagine further that the balloon has a pocked, moist inner surface and is made of exquisitely delicate material. That balloon is your lungs, and every breath you take is a miracle. What makes it possible is a thin coating of a soap-like film, or surfactant, that lowers the tension of the lung's inner surface, radically reducing the amount of force required to inhale. Without this surfactant, you couldn't breathe. "Lung surfactant is endowed with amazing biological properties," said Annelise Barron (photo), PhD, Associate Professor of Bioengineering at Stanford. "The key to this is the presence, in the surfactant, of two special proteins whose structures uniquely enable them to cut surface tension." But those same amazing structural properties, she said, also make these proteins difficult to synthesize and purify, and relatively unstable in solution, limiting shelf-life and increasing price. "One of them contains the most hydrophobic, or fat-resembling, stretch of chemical constituents of all known human proteins," Dr. Barron said.