Title |
Synthetic cationic antimicrobial peptides bind with their hydrophobic parts to drug site II of human serum albumin
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Published in |
BMC Molecular and Cell Biology, January 2014
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DOI | 10.1186/1472-6807-14-4 |
Pubmed ID | |
Authors |
Annfrid Sivertsen, Johan Isaksson, Hanna-Kirsti S Leiros, Johan Svenson, John-Sigurd Svendsen, Bjørn Olav Brandsdal |
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. |
X Demographics
Geographical breakdown
Country | Count | As % |
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United States | 1 | 100% |
Demographic breakdown
Type | Count | As % |
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Members of the public | 1 | 100% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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Japan | 1 | <1% |
Colombia | 1 | <1% |
Netherlands | 1 | <1% |
Denmark | 1 | <1% |
Unknown | 111 | 97% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 26 | 23% |
Researcher | 20 | 17% |
Professor | 12 | 10% |
Student > Bachelor | 11 | 10% |
Student > Master | 11 | 10% |
Other | 19 | 17% |
Unknown | 16 | 14% |
Readers by discipline | Count | As % |
---|---|---|
Chemistry | 27 | 23% |
Biochemistry, Genetics and Molecular Biology | 21 | 18% |
Agricultural and Biological Sciences | 18 | 16% |
Pharmacology, Toxicology and Pharmaceutical Science | 8 | 7% |
Physics and Astronomy | 3 | 3% |
Other | 13 | 11% |
Unknown | 25 | 22% |