4BKE

Recombinant human serum albumin with palmitic acid. Synthetic cationic antimicrobial peptides bind with their hydrophobic parts to drug site II of human serum albumin

Summary for 4BKE

• Entry DOI: 10.2210/pdb4bke/pdb
• Descriptor: SERUM ALBUMIN, PALMITIC ACID (3 entities in total)
• Functional Keywords: transport protein, albumin binding, group epitope mapping, molecular docking
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Secreted: P02768
• Total number of polymer chains: 1
• Total formula weight: 71264.66

Authors

Sivertsen, A.,Isaksson, J.,Leiros, H.-K.S.,Svenson, J.,Svendsen, J.-S.,Brandsdal, B.-O. (deposition date: 2013-04-24, release date: 2014-02-05, Last modification date: 2024-10-23)

Primary citation

Sivertsen, A.,Isaksson, J.,Leiros, H.S.,Svenson, J.,Svendsen, J.,Brandsdal, B.O.
Synthetic Cationic Antimicrobial Peptides Bind with Their Hydrophobic Parts to Drug Site II of Human Serum Albumin.
Bmc Struct.Biol., 14:4-, 2014

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.

PubMed: 24456893
DOI: 10.1186/1472-6807-14-4

Experimental method

X-RAY DIFFRACTION (2.35 Å)