The protein albumin is responsible for many vital processes in the human body. In nature, it only appears as a solution when dissolved in water. Chemists have developed a method of producing various albumin-based gels. Their findings might help to develop innovative drug carrier systems.
The protein albumin is responsible for many vital processes in the human body. Albumin is found in large quantities in the blood of all mammals. Human blood contains up to 60 grams per litre. In nature, it only appears as a solution when dissolved in water.
Chemists at Martin Luther University Halle-Wittenberg (MLU) have developed a method of producing various albumin-based gels. Their findings might help to develop innovative drug carrier systems that would reach the bloodstream more efficiently.
"Albumin is responsible for many important processes in the body. It can penetrate cell membranes and is thus able to transport essential substances into the cells. It also helps to detoxify cells," says Professor Dariush Hinderberger, a chemist at MLU.
"Until now albumin gels have been a somewhat annoying by-product of normal lab work," says Hinderberger. However, in the future, they could be used to produce so-called drug-delivery implants.
Albumin would be injected once into the patient and would then settle in the body. The carrier would then slowly be broken down by the body and the desired substance would be released over a longer period.This could save patients from having to undergo repeated injections.
"We wanted to find out what exactly happens to the protein particles and their structure when we modify certain properties," says Hinderberger. First, the researchers tested how the solution's pH value affects gel formation.
The liquid was then heated and analyzed to observe the changes occurred and at what stage. With the aid of infrared spectroscopy, the group was able to demonstrate how the structure of albumin changed when exposed to heat.
The protein tangle opens up allowing it to clump together with other substances to produce the gel more easily. Based on these findings the research group was able to create a different, much softer, gel.
It was done by slowing down the gel formation process, lowering the temperature and choosing a solution with relatively neutral pH value. "Hence there was a change in the structure of the albumin molecules from which the other properties of the gel stem," explains Hinderberger.
Finally, the researchers pursued the question of whether albumin gels are principally suited as drug carriers. However, follow-up studies will be needed to find out whether the substances are also suitable for pharmaceutical agents in the human body.
The study conducted by the researchers in Halle was recently featured on the cover of the International Journal Biomaterials Science published by the Royal Society of Chemistry.