The story of GFP inventions, magic markers
Mankind has not forgotten the appreciation of scientists who discovered GFP, an effective marker used in biochemical research. Osamu Shimomura, inventor of this substance killed millions of jellyfish to separate . several mg of GFP.
Chemists said that it was "a bit late " when, until this year (2008), the Nobel Prize in Chemistry was awarded for the invention of green fluorescent proteins (GFP) ).
Three scientists, Osamu Shimomura (Japan), Martin Chalfie (USA) and Roger Y. Tsien (USA, Chinese), both work in the US and are professors of the three prestigious universities of the country. public research on the nature and development of GFP applications.
Bao is late, because the first GFP was first isolated from nature in 1962, almost half a century ago. After that, it was further researched and became an effective research tool of biology and medicine.
Retrieved 50,000 jellyfish for 20 years of research to extract GFP
Osamu Shimomura, inventor of GFP substance (Photo: VNN)
In 1960, Osamu Shimomura, still a young Japanese scientist, published an article about the discovery of a glowing molecule, separated from a seafly species and was invited to the United States to work at the Biology Laboratory. studying the sea under the Department of Biology, Princeton University to continue studying the luminescence of organisms.
His object is a sea jellyfish whose scientific name is Aequorea victoria .
Over the past 20 years, every summer, Osamu Shimomura and his wife, two children - a boy and a girl - ' pilgrimage ' came to the sea to pick up jellyfish, each day over 3,000 children. When he had about 50,000 children, weighing up to 2.5 to 3 tons, he carried the ' treatment ' they used to study all year round.
In this soft and soggy creature, under the sprawling parachute there are ' hook ' muscles emitting a faint blue light. Shimomura cut those ' jaws ', squeezed them, taking the slime juice to investigate.
In addition to the number of jellyfish collected, to serve for their research, the Shimomura jellyfish were 'massacred' not less than . 1 million animals, floating in the ocean currents at Friday Harbor, Washington State on the US West Coast. He isolated the main substance in the juice, a protein with a few milligrams of efficiency in tons of jellyfish, determined its molecular formula and named it aequorin.
The sea jellyfish - Shimomura's research object
(Photo: conncoll.edu)
Shimomura then studied the mechanism of action of this substance: when combined with calcium ions it emits blue light. This light is absorbed by another protein, called GFP, in turn, emitting green light.
However, the purpose of Osamu Shimomura only wanted to understand the chemistry and biochemistry of the luminescent process in organisms, not to think about their applications later.
Thanks to GFP marking, modified observations of proteins.
GFP consists of 238 amino acids with excitation peaks (excitation peak) with wavelengths of 395 nanometers and minima - 465 nanometers. They discovered more luminescent GFP when exposed to the light of ultraviolet rays.
In the 1980s, Martin Chalfie, a professor at Columbia University, was studying the development and function of proteins in the nematode, a simple, low-order animal of only 959 cells but with a brain, also a male. children, also propagated by sexual reproduction, also . die old and have a third of the same genes as . people.
They have the advantage of being transparent so they can be tracked through a microscope but still face many obstacles. If you continue to guide this research with non-transparent animals, it is almost impossible to do so.
GFP grafted animals to study heredity.
(Photo: VNN)
Fortunately, in a seminar, he was randomly told a presentation about GFP, Martin Chalfie came up with a creative idea: why not put GFP into protein to study, to mark them and watch.
In 1992 Martin Chalfie published the achievements but the coding section of GFP into heterologous cells, for example Escherichia coli (causing diarrhea) and Caenorhabditis elegans (round worms) to turn them into luminescent luminescent bodies. green. Since then, in many laboratories around the world people have created trees that shine like fairy tales, animals like mice, rabbits, ' mythical pigs' . emitting a green light when placing them into the dark.
Along with the above research direction, people are still mutating or mutating GFP to obtain other colored GFPs. In 1995, Robert Y. Tsien at the University of California successfully performed an important denaturation method, which enhanced the spectral characteristics of GFP, had a higher luminescence intensity, and was ten times more durable.
It has taken advantage of the luminescence of GFP - used as a very specific marker - to study the processes that occur inside the cell , complex processes below the molecular level (submolecular), but before This is not visible so there is no way to track.
The achievement of creating 8-color fluorescent proteins is not to dye the animals to show up in the dark as a miracle . to prove the right to create (though it is true!) To observe 8 biological processes are taking place at a time, determining the role of 8 proteins simultaneously in one body, both understanding the interactions between them, while shortening the study time many times.
GFP color spectrum can be used to mark proteins in research.(Photo: VNN)
By introducing GFP into protein, based on their observations by light emitted by them, it is possible to understand the function and metabolism of each protein in the body, serving the basic understanding of humans. (as well as other plants and animals).
It is roughly comparable that this is similar to attaching an electronic chip that signals a specific parameter to a wild animal and then releases it freely in the jungle, then sitting still can know where it is, what it is doing or is in danger to respond promptly. GFP's role is the same, but much more subtle.
In its announcement, the Royal Swedish Academy wrote: Luminescent proteins ' during the past decade have functioned as a guiding star for biologists, biochemists, and medical researchers. and other scientists'.
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