PEPTIDE SELF-ASSEMBLY BIOMATERIALS DESIGN AND APPLICATION - Biologically-Responsive Hybrid Biomaterials - page 80

membrane proteins because removal of lipids from membrane proteins affects
protein solubility and conformational stability. Despite a variety of detergents
and lipids behaved as surfactants has been used to solubilize, stabilize, purify and
crystallize membrane proteins over decades, the way surfactants interact with
membrane proteins to influence structure and function and therefore criteria for
choosing good surfactants remain largely unknown. This is partly due to the
complexity of membrane protein-detergent-lipid interactions and lack of a
“magic material” surfactant. Hence the need to develop new membrane
compatible material is acute [16, 17] .
Fig. 6. A proposed model for the lipid-like peptides to stabilize membrane proteins. These simple
self-assembling lipid-like peptides have been used to solubilize, stabilize, and crystallize membrane
proteins. These peptides have a hydrophilic head and a hydrophobic tail, much like other biological
lipids. They use their tail to sequester the hydrophobic part of the membrane proteins, and the
hydrophilic heads are exposed to water. Thus, they make membrane proteins soluble and stable
outside of their native cellular lipid milieu. These lipid-like peptides are very important for
accelerating determination of the high resolutions of molecular structure for challenging membrane
proteins.
These simple designer peptide surfactants may now open a new avenue to
overcome one of the biggest challenges in biology: not only to obtain large
numbers of high-resolution structures of membrane proteins and but also to
understand their important biological functions.