Download MendeleySynthetic Cationic Antimicrobial Peptides Bind with Their Hydrophobic Parts to Drug Site II of Human Serum Albumin.
Sivertsen, A., Isaksson, J., Leiros, H.S., Svenson, J., Svendsen, J., Brandsdal, B.O.(2014) BMC Struct Biol 14: 4
- PubMed: 24456893
- DOI: https://doi.org/10.1186/1472-6807-14-4
- Primary Citation of Related Structures:
4BKE - PubMed Abstract:
Many biologically active compounds bind to plasma transport proteins, and this binding can be either advantageous or disadvantageous from a drug design perspective. Human serum albumin (HSA) is one of the most important transport proteins in the cardiovascular system due to its great binding capacity and high physiological concentration. HSA has a preference for accommodating neutral lipophilic and acidic drug-like ligands, but is also surprisingly able to bind positively charged peptides. Understanding of how short cationic antimicrobial peptides interact with human serum albumin is of importance for developing such compounds into the clinics.
Organizational Affiliation:
The Norwegian Structural Biology Centre, Department of Chemistry, Faculty of Science and Technology, University of Tromsø, NO-9037 Tromsø, Norway. bjorn-olav.brandsdal@uit.no.
