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Space Station: High-value Drug Research

Mastering microgravity. Research onboard the International Space Station. Credit: NASA

Set for an upcoming ride to the International Space Station (ISS) are nearly a100 proteins to be used in crystallization studies – microgravity research that could lead to innovative methods of drug discovery.

A SpaceX Falcon booster is to depart Florida on March 16, making a delivery run to the orbiting complex.

The protein crystallization research is being pursued by the University of Alabama at Birmingham’s (UAB) Center for Biophysical Sciences and Engineering (CBSE).

Scientists with the CBSE have been interested in microgravity research for years. Research has shown that many proteins flown in space demonstrated the propensity to grow crystals with an increased size and quality compared to crystals grown in a lab on Earth.

“Understanding the atomic structure and function of a protein allows scientists to begin development on compounds that can interact with the protein and subsequently regulate its function,” said Lawrence DeLucas, director of the CBSE.

Microgravity: a valuable resource?

DeLucas is a former NASA astronaut. He performed his own protein crystallization experiments on board the STS-50 space shuttle flight (June 25-July 9, 1992).

The ISS-grown crystals will be compared to control experiments performed at UAB. Researchers from across the United States have contributed their protein samples for flight. These proteins will remain on the space station until August, when they return to Earth.

The goal of the experiment is to demonstrate whether microgravity is a valuable resource for improving the quality of a protein crystal, DeLucas said in a UAB press statement.

Structure-based drug design

Analyzing a resulting protein crystal includes X-ray diffraction, whereby the crystal form of the protein is subjected to an X-ray beam.

The X-rays create a pattern of all the amino acids in the protein that scientists then use to create models for drug design. X-ray crystallography is considered by many to be the optimal method for evaluating protein crystals.

This method, utilized in university and pharmaceutical laboratories, is often referred to as structure-based drug design, and it has contributed to development of a multitude of drugs to treat cancer, HIV, diabetes, and other chronic and infectious diseases.

“There are many projects with proteins that are considered high-value drug targets that have been unable to grow diffraction-quality crystals,” DeLucas said. “We would like to determine whether microgravity can play a role in overcoming such obstacles found in structure-based drug discovery.”

By Leonard David

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