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Titolo:
Effect of antimicrobial apomyoglobin 56-131 peptide on liposomes and planar lipid bilayer membrane
Autore:
Mak, P; Szewczyk, A; Mickowska, B; Kicinska, A; Dubin, A;
Indirizzi:
Jagiellonian Univ, Inst Mol Biol, PL-31120 Krakow, Poland Jagiellonian Univ Krakow Poland PL-31120 l Biol, PL-31120 Krakow, Poland Polish Acad Sci, M Nencki Inst Expt Biol, Lab Intracellular Ion Channels, PL-02093 Warsaw, Poland Polish Acad Sci Warsaw Poland PL-02093 Channels, PL-02093 Warsaw, Poland
Titolo Testata:
INTERNATIONAL JOURNAL OF ANTIMICROBIAL AGENTS
fascicolo: 2, volume: 17, anno: 2001,
pagine: 137 - 142
SICI:
0924-8579(200102)17:2<137:EOAA5P>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANTIBACTERIAL ACTIVITY; IDENTIFICATION; RESISTANCE;
Keywords:
antimicrobial peptides; haemocidins; haem-binding proteins; planar lipid bilayer; liposomes;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Dubin, A Jagiellonian Univ, Inst Mol Biol, 3 Mickiewicza Ave, PL-31120 Krakow, Poland Jagiellonian Univ 3 Mickiewicza Ave Krakow Poland PL-31120 oland
Citazione:
P. Mak et al., "Effect of antimicrobial apomyoglobin 56-131 peptide on liposomes and planar lipid bilayer membrane", INT J ANT A, 17(2), 2001, pp. 137-142

Abstract

The horse apomyoglobin 56-131 peptide is a convenient object for studies on the recently discovered antimicrobial activities of haem-binding protein fragments called haemocidins. The purpose of this study was to determine the effect of this peptide on planar lipid bilayer membranes and on liposomesof different lipid compositions. Micromolar concentrations of the apomyoglobin 56-131 fragment disrupt phosphatidylserine/phosphatidylethanolamine planar lipid bilayers without discrete conductance changes. The observed detergent-like action is dependent on peptide concentration: the lower amount of peptide resulted in longer bilayer lifetime. The cholesterol has an inhibitory effect on peptide-induced liposome lysis as shown by calcein release from liposomes. Additionally, there was considerable lytic activity on liposomes formed from anionic lipids of the sort found in bacterial membranes. Circular dichroism (CD) experiments showed that the peptide had a disordered structure in aqueous solutions and folds gradually to form helices in both membrane-mimetic trifluoroethanol solutions as well as in liposome suspensions. The features of the apomyoglobin 56 131 fragment that are similar tothe cationic antimicrobial peptides acting in a 'carpet-like' manner are discussed. (C) 2001 Elsevier Science B.V. and International Society of Chemotherapy. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 22:17:46