Extracellular cross links

All the proteins in our cells are replaced quite regularly because they get damaged. But some of the proteins outside our cells aren’t replaced or only very slowly. The working is often very simple, so a minor change isn’t that serious. But after a while it can cause problems. Mostly they have a biophysical function like give a tissue elasticity (for example the artery wall) or high tensile strength like the ligaments or transparency like the lens of the eye. A good example of one of the problems which extracellular cross links is the case of the artery wall which becomes more rigid and leads to high blood pressure. When two proteins in our artery wall bond together (cross-linking) then they loose there ability to slide across or along each other. Luckily, a lot of these structure have very unusual chemical structures, not found in proteins our other molecules that the body makes on purpose. This means that it’s possible to make molecules that break these cross links without reacting which other molecules that your body needs. One of these cross-links breakers is ALT-711, today known as alagebrium chloride. But there are cross-links that alagebrium chloride can’t break, so we need to develop some other cross-link breakers too. A problem is that some molecules are too stable to be broken down by a non-toxic small molecule. Maybe you will ask yourself: “why can toxic molecules break it while non toxic can’t”. Well this is because some toxic molecules our very reactive and will not only beak the cross-link but also the rest of the molecules inside your body. The solution for this problem can be the creation of enzymes that can break these cross-links or other molecules that bound to stable molecules but inactivate themselves when they are bounded. Alagebrium chloride can also beak down glycolysation end-products (A.G.E.s).