Structure-activity studies on magainins and other host defense peptides
| Autor: | W L Maloy, U P Kari |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Insecta
Ranidae Molecular Sequence Data Antimicrobial peptides Biophysics Moths Biochemistry Microbiology Biomaterials chemistry.chemical_compound Horseshoe Crabs medicine Animals Amino Acid Sequence Pathogen Peptide sequence Mammals chemistry.chemical_classification Sequence Homology Amino Acid biology Diptera Organic Chemistry Magainin General Medicine Antimicrobial biology.organism_classification Anti-Bacterial Agents Amino acid chemistry Mechanism of action Insect Hormones medicine.symptom Peptides Bacteria |
| Zdroj: | Biopolymers. 37:105-122 |
| ISSN: | 1097-0282 0006-3525 |
| DOI: | 10.1002/bip.360370206 |
| Popis: | Host defense peptides are widely distributed in nature, being found in species from bacteria to humans. The structures of these peptides from insects, horseshoe crabs, frogs, and mammals are known to have the common features of a net cationic charge due to the presence of multiple Arg and Lys residues and in most cases the ability to form amphipathic structures. These properties are important for the mechanism of action that is thought to be a nonreceptor-mediated interaction with the anionic phospholipids of the target cell followed by incorporation into the membrane and disruption of the membrane structure. Host defense peptides have been shown to have broad spectrum antimicrobial activity, able to kill most strains of bacteria as well as some fungi, protozoa, and in addition, many types of tumor cells. Specificity for pathogenic cells over host cells is thought to be due to the composition of the cell membranes, with an increased proportion of anionic phospholipids making the pathogen more susceptible and the presence of cholesterol making the host membranes more resistant. Structure-activity relationship studies have been performed on insect cecropins and apidaecins, horseshoe crab tachyplesins and polyphemusins, and the frog magainins, CPFs (caerulein precursor fragments) and PGLa. In general, changes that increased the basicity and stabilized the amphipathic structure have increased the antimicrobial activity; however, as the peptides become more hydrophobic the degree of specificity decreases. One magainin-2 analogue, MSI-78, has been developed by Magainin Pharmaceuticals as a topical antiinfective and is presently in clinical trials for the treatment of infected diabetic foot ulcers. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text