Huge Steps in Glycomics & Glycobiolgy

As defined on our web site, glycobiology "refers to the study of biological sugars". Glycomics encompasses the method by which these sugars are studied.

For years we have known about genetics which is the study of genes. We have also known about proteomics which is the study of proteins. These fields are extremely complicated to understand but incredibly easy to study in the sense that DNA and protein sequences can (and have been for many years) be synthesized because of molecule association.

Let me explain. DNA has three major components:

1. Deoxyribose (a 5-carbon sugar; D in DNA)
2. Phosphate (creates bond between deoxyribose molecues to form backbone)
3. Nucleic Acids (A, C, G, T; NA in DNA)

A is for adenine, C for cytosine, G for guanine, T for thymine. Hydrogen bonds between these four nucleotides hold DNA's double helix together as can be seen in this picture:


Pay close attention and you will notices that a big nucleotide (purine) always binds to a small nucleotide (pyrimidine). The specificity goes into even more exactitude! Not only can you predict that an A and G will always bind to a C or T, but you can predict that an A will ALWAYS bind to a T and a G will ALWAYS bind to a G. That's just the way it is. In DNA, no other nucleotides are present and other combination exists. Geneticists can fairly easily (although concept or procedure might be complex for non-biologists).

The same predictability is true in the study of proteins (proteomics). An amino acid has two end points which can attach to other amino acids to form (not fold) an oligopeptide, a true peptide, or a protein. Here is a list of the 20 amino acids in the human body:


Do you see the H₃N⁺ and COO^- at the top of each of the diagrams? The amino group (H₃N⁺) from one amino acid will ALWAYS bind to the carboxylic acid group (COO^-) of another. The only exception is when folding, other interactions can occur between sides groups but the protein backbone (line of H₃N⁺ to COO^-) linkages between amino acids) is not modified during fold/unfolding. Again, having a predictable pattern for linkage has facilitated the creation of proteins in labs for research purposes.

Sugar on the other hand has no such predictability... Or at least it didn't. Yesterday, ScienceDaily reported that scientists from the University of Georgia had found a way to synthesize complex carbohydrate structures in a much faster, more accurate process than ever before.

Why is this important?
Direct quote from article:
"The emerging field of glycomics has been severely hampered by a lack of robust, well-defined libraries of carbohydrate molecules, which are greatly needed to decipher the 'carbohydrate codes' used by cells for processes such as cell signaling, embryogenesis and neuronal development," said Pamela Marino, director of the glycobiology portfolio at the NIH's National Institute of General Medical Sciences.

This article linked to a similar article (March 23, 2009) in which German scientists boasted of having created "a device that builds these intricate [sugar] molecules in a few hours — rather than the months or years required with existing technology." This second article talks about the direct links to possible vaccines and medications that can spawn from this advancement.

Article [ScienceDaily]: New Method for Producing 'Libraries' of Important Carbohydrate Molecules
Article [ScienceDaily]: First Automated Carbohydrate 'Assembly Line' Opens Door To New Field Of Medicine

It's time you look at sugar a different way. Not all sugar is sucrose (table sugar) or glucose (fuel source and responsible for insulin secretion). No... Instead, glycobiology has been referred to by many prominent doctors as the latest frontier in medical and scientific research. To learn more about it, visit our site. Glyconutrients are eight essential sugars commonly found on surfaces of cells in the human body.

Glycobiology & Synthetic Bacteria

For years we have said that the future of medical and health-related research is in the study of sugars and sugar-containing molecules (ie. glycoproteins, glycolipids, etc.).

"Researchers have devised a way to attach sugars to proteins using unique biological and chemical methods. This means that large quantities of different glycoproteins can be generated for various medical and biological studies."

Recently, a paper was published in the journal Nature Chemical Biology in which it was reported that a bacteria (Campylobacter) could do something that was believed could only be done by animal/plant cells (eukaryotes). E. coli has always been used for research but is unable to glycosylate (add monosaccharides to other molecules).

"PhD student Flavio Schwarz from Professor Markus Aebi's group at the Institute of Microbiology of ETH-Zurich and researchers from the University of Maryland have developed a new method for producing glycoproteins." They have taken the glycosylation mechanism from Campylobacter and introduced it to E. coli. E. Coli will now be able to glycosylate.

What is so important about glycosylated molecules like glycoproteins?
"If you want to study host-pathogen interactions, for instance, you need pure samples of a particular glycoprotein, whereas natural systems can only offer researchers a highly complex blend of such substances." ALL pathogens interact and attach to human cells through carbohydrates on glycosylated structures.

"Glycoproteins play a crucial role in biology. They are found more frequently on the surface of cells than 'normal' proteins and they participate in numerous cellular processes, such as cell to cell communication. They are present throughout the human body, also in mucus, and the different glycosylation of blood proteins contribute to define the blood group antigen." Cell to cell communication is also called intercelullar communication.

What does the future hold?
"...has great potential for the development of new cancer treatments. These therapeutic glycoproteins can be produced specifically-tailored to remain in the bloodstream longer while targeting cancerous cells." The immune system uses glycoproteins to distinguish between rogue and normal cells.

"For now, we have simply managed to prove that our concept works. It remains to be seen what potential practical applications it might have," says Flavio Schwarz from the Life Science Zurich Graduate School."

Article [ScienceDaily: Synthetic Biology: Engineered Bacteria

Related Information
Glyconutrientes
Glycobiology
Essential Monosaccharides
Intercellular Communication