Atomic force microscopy: A multifaceted tool to study membrane proteins and their interactions with ligands

Abstract

Membrane proteins are embedded in lipid bilayers and facilitate the communication between the external environment and the interior of the cell. This communication is often mediated by the binding of ligands to the membrane protein. Understanding the nature of the interaction between a ligand and membrane protein is required to both understand the mechanism of action of these proteins and for the development of novel pharmacological drugs. The highly hydrophobic nature of membrane proteins and the requirement of a lipid bilayer for native function have hampered the structural and molecular characterization of these proteins under physiologically relevant conditions. Atomic force microscopy offers a solution to studying membrane proteins and their interactions with ligands under physiologically relevant conditions and can provide novel insights about the nature of these critical molecular interactions that facilitate cellular communication. In this review, we provide an overview of the atomic force microscopy technique and discuss its application in the study of a variety of questions related to the interaction between a membrane protein and a ligand.

The physics of pulling polyproteins: a review of single molecule force spectroscopy using the AFM to study protein unfolding

“…Membrane proteins and their interactions with ligands have been extensively studied by SMFS techniques [22,23]. We would like to point our readers to specific reviews on the single molecule force spectroscopy of membrane proteins for more detailed information about the recent contributions SMFS has had to this class of protein [24][25][26][27][28].…”

Optimizing the calculation of energy landscape parameters from single-molecule protein unfolding experiments

“…A recent review provides details of studies that have employed the Zhurkov-Bell model to extract parameters of the unfolding energy landscape of a protein from experimental data on polyproteins [43]. In addition, since that review, 12 additional studies have used the Zhurkov-Bell model to extract information from force spectroscopy experiments [15,[44][45][46][47][48][49][50][51][52][53][54]. Given the prevalence of the Zhurkov-Bell model in force spectroscopy experiments, it is interesting to examine its application and accuracy in more detail.…”

The effect of vasonit on the structural/functional state of erythrocyte cytoplasmic membrane in patients with ischemic stroke

“…Их действие основано на способности некоторых материалов изменять геоме-трические размеры под действием электрического напря-жения. Подавая на электроды таких пьезоэлектрических манипуляторов соответствующее напряжение, можно осуществлять заданное механическое перемещение с точ-ностью до доли ангстрема [8][9][10][11]. На сегодняшний день в литературе не встречаются описания исследований влия-ния пентоксифиллина на упруго-вязкостные свойства мембраны эритроцитов методом АСМ.…”