Yes it is possible if u know the prior information about the receptor molecule which u want to express. It much contains the signal peptide to direct the receptor molecule to proper location or surface on the cell.
It takes a lot of expertise and engineering to design a whole new receptor which doesn't already exist in any biological medium. But if you successfully design such receptor (which is an extremely demanding task), there are a handful of methods to place it on cell surfaces depending on its structure.
If you want to do something like a completely new receptor you may be need to think if your receptor will be expressed all the time or in response to some stimuli. And how your receptor will be addressed and maintain on the membrane and if it's a metabotropic one which are the second messengers. Because if you create a receptor even if this receptor is expressed you will never see the function of your receptor if this one is not on the membrane!
All these thinks together will give one big part (impossible to change) of your receptor!
Hi, Read about chimeric antigen receptors (CARs) which genetically engineered T cell receptors. These are artificial receptors on T cells that have constructed in order to enhancing T cell specificity.
Could you give us a little more information? Are you wanting to generate a stable cell line which expresses this 'artificial receptor?' Would transient expression of the receptor be acceptable? Are you thinking of a receptor that has been mutated or altered slightly or are you thinking of introducing an entirely new receptor to a cell?
I think I did mistake your question. I think you are asking if it is possible for a cell to bind a drug in long term contact - when normal experiments show that it does not APPEAR to have a receptor for the drug. In this case the drug is alginate film.
Very important is to define how tight the "new" binding is. Do the cells now bind tightly enough that they cannot be washed from the drug? Is there a sufficiently low Kd value? How long does EQUILIBRIUM take?
The answer is absolutely yes. This does not mean a receptor was "generated". It can be explained by many phenomena grouped under "non-specific" binding. However,
1. If say you put 1000 cells, and 10 cells remain bound = 1% I would call it non-specific. If 100 cells out of 1000 bound then = 10%, I would still call it non-specific but somewhat high non-specific binding - upto 20% would be a maximum. After 25% I would seriously look on reducing this non-specific binding.
2. If 500 out of 1000 cells bound = 50%, then your ORIGINAL HYPOTHESIS is wrong. You cannot assume a receptor was "created", but that your cells bind the drug or alginate film. See further below:
3. Now let us look at an time course. You wash cells on day 1 and only 1% bind. Then the cells do not bind alginate.
** On day 2 in a separate sample you get 5% binding - this is fine.
** But by day 5, 50% of cells are bound. Then you have a problem:
a. One case is non-specific binding increases with contact - the equilibrium time required for NON-specific binding can be long. YOU MUST then determine what is the equilibrium time for A SPECIFIC drug/cell binding. If this is day 1 giving you 100% binding then it is non-specific on day 5.
BUT what is non-specific if at day 5 50% binds. THEN degradation, denaturation, change in medium pH, ionic strength etc. etc. all have to be checked BEFORE you worry about a receptor. This is CRITICAL.
b. If the cells are viable and slow growing, then binding CAN induce new proteins on day 5, not seen on day 1. Only in this case, you can say there is a receptor "created" or induced. BUT then you have to prove it that new proteins are induced on the cell surface. That is much less easy !