To make monolayers of proteins in the aqueous phase, I need to dissolve proteins in organic solvent. Is there a method without affecting protein structure too much?
Any method such that the protein structure can get back function later after the
solvent evaporates would be nice. Thanks
You can try to solubilize your protein in "reverse micelles" using special detergents such as AOT (di-octylsulfosuccinate). There is a whole body of literature on how to approach such experiments, just search for "reverse micelles" and / or "AOT".
Some proteins / enzymes tolerate this better than others, but it always depends on what type of organic solvent you use.
Hi Thanga, are you working with a single protein or a protein mixture? Proteins vary considerably in their stability in organic solvents.
Also, can you use your proteins dissolved in di H2O containing volatile buffers?
There have been studies of enzymatic catalysis in organic solvents. See this paper for example:
http://www.ncbi.nlm.nih.gov/pubmed/11751059
if you want to make monolayers at the air-water interface there is no need for organic solvent. Just change the ionic strength of the subphase and using the salting out effect the enzyme will be stable.
Plenty of work published on that in the literature.
I agree with @Jhony. I have applied aqueous solutions of many different proteins and peptides successfully to the air-water interface of a Langmuir-Blodgett trough using a Hamilton syringe (mounted on a stabilizing stand). In my case, the water sub-phase was physiological pH and ionic strength.
One example is
Article Synthesis and biophysical characterization of engineered top...
- Badges
- Science topic
- Similar topics
- Biological Science
- Molecular Biology