Nothing Special   »   [go: up one dir, main page]

Lesson 4.2. Glycoconjugates

Download as pdf or txt
Download as pdf or txt
You are on page 1of 4

Lesson 4.

2: Glycoconjugates
Lesson Summary
This lesson will discuss the different association of carbohydrates with other non-carbohydrate
molecules. This will also discuss the importance and functions of glycoconjugates.

Learning Outcomes
At the end of this lesson, the student should be able to:

1. Identify the different types of glycoconjugates, and

2. Discuss the occurrence, importance and functions of glycoconjugates.

Motivation Question
What are other molecules attached to carbohydrates?

Discussion
Glycoconjugates

Glycoconjugate is a molecule of carbohydrates covalently bonded with other biomolecules such


as proteins and lipids. Most of the carbohydrates in glycoconjugates are oligosaccharides. The
oligosaccharides in glycoconjugates may serve a structural function, for reactivity and surface
recognition. As a hydrophilic molecule oligosaccharide has a good structural function for protein
surfaces. In terms of reactivity, oligosaccharides may shield the surface and thus affect
reactivity. Also, oligosaccharides may serve as label such as in label proteins and also serves
as intracellular communication.

Glycolipids

Glycolipids are glycoconjugates of carbohydrates and lipids and is common among membrane
lipids.

The lipids are generally hydrophobic (water fearing) and the oligosaccharides are hydrophilic.
Glycolipids generally serve as a surface recognition site.
Figure 55. Structure of glycolipids

Glycoproteins

Glycoproteins are glycoconjugate of proteins and carbohydrates and has a wide variable
composition (microheterogeneity). It also has a large array of functions such as for structure,
transport, enzymes, receptors, etc. The carbohydrate chains are often short (oligosaccharides),
though not all, and may be branched. The carbohydrate moiety is synthesized by enzymatic
reaction and covalently linked to polypeptide (protein component).

Examples of glycoprotein are the proteoglycans and peptidoglycan. Proteoglycans are


extracellular aggregate of protein and glycosaminoglycans. It has a core protein where the
carbohydrate unit will form a glycosidic bound to the oxygen of the serine or threonine amino
acids in the core protein. Proteoglycan aggregates also has a single hyaluronoate molecule
backbone.

Peptidoglycan is a glycoprotein of covalently linked polysaccharide and polypeptide chain and is


common among bacterial cell wall. With these linking, the amino acids in the protein component
can resist hydrolysis by peptidases making it invulnerable by degrading enzymes. However, this
can be broken down by the lysozyme. Peptidoglycan made certain bacteria resistant to several
harmful factors. Penicillin was proven to inhibit the cross-linking of the polysaccharides and
polypeptides, or the synthesis of the peptidoglycan. However, through time, Bacteria developed
a resistance with penicillin.

Glycoproteins serve several biological importance aside from its structural functions. It also acts
as surface recognition, specifically the carbohydrate component, such as the syndecan.
Syndecan are human membrane core protein with heparan sulfate carbohydrate units.
Figure 56. Glycoproteins embedded in the plasma membrane

This glycoprotein plays a very important role in the prevention of blood clot. The carbohydrate
unit in this glycoprotein has a sulfated monosaccharide chain (NS domain) which is serves as
binding site for the antithrombin (AT) molecule.

Figure 57. The sulfated domain in the oligosaccharide of heparan sulfate

Figure 58. The binding of AT to the S domain lading to the conformational change for factor Xa to attach

In the presence of the sulfated monosaccharide chain in the glycoprotein, the protein
antithrombin will attached causing it to have a conformational change in its structure. This
conformational change of the antithrombin will allow its interaction with Factor Xa, a blood
clotting factor. Without the conformational change of AT, due to its binding to the sulfated
carbohydrate moiety in syndecan, factor Xa cannot bind to AT thus uncontrolled bleeding may
occur.
On the other hand, if thrombin and antithrombin molecules are present, it will bind to two
adjacent NS domains in the heparan sulfate bringing the two proteins in closer proximity which
will lead to its interaction. The attached thrombin to the AT will inhibit the interaction of factor Xa.
In this case blood clotting will be inhibited.

Figure 59. Interaction of thrombin to antithrombin inhibiting the attachment of factor Xa

You might also like