For the first time, scientists at Johns Hopkins University drew a "stability map" for enzymes in cell membranes, revealing the important morphological maintenance and functional areas of this enzyme. The research has been published in the online version of Structure magazine and Nature Chemical Biology. The researchers hope to promote the treatment of malaria and other parasitic diseases through their research.
"This is the first time to truly understand the architectural logic behind this enzyme structure," said Dr. Sinisa Urban, associate professor of molecular biology and genetics at the Johns Hopkins University School of Medicine. His research team has identified a special enzyme located in the cell membrane, the rhomboid rhomboid. Proteases were studied.
Intramembrane proteases hydrolyze peptide bonds in cell membranes, a process that is ubiquitous in all life types and involves a variety of diseases. It is necessary to break the structural support behind the proteolysis in the cell membrane. The diamond-shaped protease present in various organisms is located in the cell membrane, where it functions as a cleavage protein.
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Previous research by Urban and colleagues showed that diamond proteases are critical for the malaria-causing Plasmodium falciparum, which can help them successfully invade red blood cells and eventually lead to infection. The researchers believe that understanding the stability of the rhombic protease form will help develop inhibitors of this enzyme as therapeutic drugs. "There are currently no corresponding selective inhibitors of rhomboid proteases," Urban said. "We really need to understand the mechanism of action of this enzyme. Is it as hard as stone or as elastic as jelly?" BioCom
The challenge with diamond-shaped proteases is that the enzyme is surrounded by cell membranes, making it difficult for researchers to manipulate. To this end, Urban's research team adopted a light scattering technology called thermal light scattering, which can detect the light bounced back by the molecule while gradually warming the enzyme sample. Once the normal structure of the enzyme is destroyed, its scattered light will be different, and the temperature at this time (that is, the breaking point of the enzyme) reflects the intrinsic stability of the enzyme.
The researchers accurately tested the stability of the E. coli diamond protease. Surprisingly, this enzyme is "more like jelly" than other membrane proteins with similar morphology. The researchers believe that this characteristic helps rhomboids interact with the proteins they cleave. The researchers synthesized 150 different versions of rhomboid proteases, and conducted separate studies to understand which of the rhomboid proteases are important regions for morphological maintenance, and which regions are essential for their hydrolysis function. They found four main areas to maintain the morphology and two important functional areas.
Subsequently, the researchers used computer simulations to analyze diamond proteases. They incorporated the characteristics of the natural membrane environment in the computer model of the rhomboid protease. These characteristics include mainly composed of lipids and extremely limited water content. The computer program then simulated the effect of this environment on diamond proteases. The researchers found that the diamond-shaped protease has a special internal area where water molecules can be stored. This is a major advantage for this protein hydrolyzing enzyme in an environment with limited water content.
"This makes us very excited. In addition, some rhombic proteases that have no obvious change in stability or morphology have lost their function. We are also very curious about this," Urban said. He hopes that a better understanding of diamond proteases can help guide the development of new drugs for malaria and other parasitic diseases.
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