User:Sanjaygkp

Amphiphilic peptides have been shown to form defined nanostructures such as molecular wires, well defined nanotubes as well as nanovesicles. Advances made in the synthesis of amphiphilic peptides during the past few years, allows for their use as scaffolds for the synthesis of defined nanometer structures. Extensive studies of biological systems on the molecular level in the 20th century revealed that molecular self-assembly is a fundamental process in all living systems. Specifically, proteins that form the primary components of the molecular machinery that allows life to exist have a vast array of resources available to allow them to self-assemble. However, it also has been observed that the aberration of protein self-assembly is often the cause of severe, progressive human diseases that can have a serious social impact. Small organic molecules as well as peptides possessing both, hydrophilic and hydrophobic moieties can bind other peptides or protein molecules through hydrogen bonds and hydrophobic interactions and are behind the driving forces for molecular self-assembly.