Biochemists create protocells to explore how lipids may have led to first cell membranes







A team of biochemists at the University of California, San Diego, working with a group of biochemical engineers from the University of California, Los Angeles, has found that the development of short lipids might have led to the development of the first cell membranes on early Earth.

In their study published in the journal Nature Chemistry, the group combined cysteine with chemical relatives of fatty acids to form lipids with two tails, finding clues about the origins of life on Earth.

The research team reasoned that for cells to get their start on early Earth, some form of cell boundary must have formed first to protect cell contents from the environment. Noting that modern cell membranes are all made of lipids, the researchers wondered if the first cell membranes might have been made of lipids as well—and if that was the case, how they might have developed from simple molecules.

They also noted that modern cell membranes are complex and generally long chained. Suspecting that early-life molecules would have had simpler membranes, they wondered if they might have been made of short fatty acids.

To find out, the team started with cysteine, an amino acid that they had previously identified as likely prevalent during the earliest days of the planet, serving as a glue of sorts, holding precursor molecules together.

They combined the amino acid with short fatty acids with eight carbon atoms. During combination, the molecules reacted, forming a lipid—one with two tails. They noted that some of them also self-formed into spheres with membranes, which the team dubbed protocells. The spheres lacked any of the compounds found in living cells, of course, but did appear to be capable of serving as a sort of staging ground.

The researchers also saw that the protocell membranes were aligned in a double layer and the spheres showed signs of being able to corral other molecules inside of them, allowing for the admission of other components for the development of life. Their protocells were robust enough to survive mixing with the magnesium and calcium ions that would most likely have been plentiful on early Earth.

According to the researchers, the work shows a possible means for the development of cell membranes on early Earth, making the path toward the development of life possible.


Website: Global Innovation Technologist Awards

#Biochemistry #Sciencefather #Research award #MolecularBiology, #Proteomics, #Metabolomics, #EnzymeKinetics, #CellBiology, #BiochemicalResearch, #ProteinStructure, #Genomics, #BiochemicalEngineering, #StructuralBiology, #SystemsBiology, #BiochemicalPathways, #ChemicalBiology, #Bioinformatics, #Pharmacology, #DrugDesign, #BiochemicalAnalysis, #MetabolicPathways #Professor, #Lecturer, #Scientist, #Scholar, #Researcher, #Analyst, #Engineer, #Technician, #Coordinator, #Specialist, #Writer, #Assistant, #Associate, #Biologist, #Chemist, #Physicist, #Statistician, #DataScientist

Visit Our Website : innovationtechnologist.com

Get Connected Here:
==================
Social Media Link

Comments

Post a Comment

Popular posts from this blog

From chaos to order: Proteins can re-structure themselves to create important substances

Image
The protein 'MIPS' changes its internal structure when it becomes active. Its disordered active centre becomes a defined structure with special functions. The protein plays a key role in the production of inositol, which is also known as vitamin B8, and fulfils important tasks in the body. Researchers at Martin Luther University Halle-Wittenberg (MLU) and the National Hellenic Research Centre in Greece have succeeded for the first time in observing the protein as it re-structures. As the team reports in the scientific journal 'Proceedings of the National Academy of Sciences' (PNAS) this process appears to occur in many similar proteins. Proteins control all vital processes in every organism, for example growth and metabolism. A basic principle of protein research is that the structure of each protein determines its function. If the structure is impaired at just one specific point, the protein can no longer fulfil its function. In the human body, this can lead, for exam...
Read more

Amie Boal named Nicholas and Gelsa Pelick Family Chair in Science

Image
UNIVERSITY PARK, Pa. — Amie Boal, professor of chemistry and of biochemistry and molecular biology, has been named the Nicholas and Gelsa Pelick Family Chair in Science . The purpose of the endowed faculty chair is to provide an outstanding biochemist in the Department of Chemistry or the Department of Biochemistry and Molecular Biology with the resources needed to continue and further their contributions to research , teaching and public service. “I am extremely pleased that we can recognize Amie’s accomplishments and many contributions to Penn State with this well-deserved appointment,” said Mary Beth Williams, acting dean of the Eberly College of Science, James and Alvina Balog Faculty Fellow in Science , and professor of chemistry . “Amie was chosen for her exceptional research , teaching and service to the Department of Chemistry and the Eberly College of Science. She is an integral part of the college’s commitment to excellence and I’m certain that will continue with this new ap...
Read more