Activity: Talk or presentation › Invited talk › unknown
Description
Single biomolecules (e.g. antibodies) are able to specifically recognize and bind their corresponding partner with high efficiency. This process is known to play a pivotal role in biology, physiology and medicine. From the chemical point of view bio-recognition can be described as a combination of non-covalent weak interactions including electrostatic (ionic), hydrophobic, and van der Waals interactions as well as hydrogen bonding. Furthermore, steric aspects, especially the complementary structure of the two binding partners, are highly relevant for complex formation and stability. Taken together all these aspects determine both, the strength and the characteristic lifetime of the bond. To determine receptor ligand interactions on the molecular level, the atomic force microscopy (AFM) based molecular recognition forces spectroscopy (MRFS)1 offers the most versatile approach to explore forces during the bio-recognition processes at the molecular level. In MRFS the tip of an AFM cantilever is upgraded to a molecular biosensor2 resulting in a single ligand molecule tethered at the outer tip apex, which is allowed to interact with its corresponding binding partner (e.g. isolated proteins3, artificial4 or native biomembranes5 or living or fixed cells6). As a result, molecular interaction forces and complete energy landscapes can be explored, gaining insights into structure and function of nanomedical relevant receptor-ligand pairs.
Period
10 Nov 2015
Event title
Surface Modification for Chemical and Biochemical Sensing - SMCBS 2015