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> (2000-2009)
> Schmidtchen Artur
> Malmsten Martin 1964 >
Oligotryptophan-tag...
Oligotryptophan-tagged antimicrobial peptides and the role of the cationic sequence
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- Strömstedt, Adam A., 1977- (author)
- Uppsala University,Uppsala universitet,Institutionen för farmaci,Pharmaceutical Physical Chemistry
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- Pasupuleti, Mukesh (author)
- Lund University,Lunds universitet,Dermatologi och venereologi, Lund,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Dermatology and Venereology (Lund),Section III,Department of Clinical Sciences, Lund,Faculty of Medicine,Department of Clinical Sciences, Lund University,Dermatology and Venereology
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- Schmidtchen, Artur (author)
- Lund University,Lunds universitet,Dermatologi och venereologi, Lund,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Dermatology and Venereology (Lund),Section III,Department of Clinical Sciences, Lund,Faculty of Medicine,Department of Clinical Sciences, Lund University,Dermatology and Venereology
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- Malmsten, Martin, 1964- (author)
- Uppsala University,Uppsala universitet,Institutionen för farmaci,Pharmaceutical Physical Chemistry
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(creator_code:org_t)
- Elsevier BV, 2009
- 2009
- English.
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In: Biochimica et Biophysica Acta - Biomembranes. - : Elsevier BV. - 0005-2736 .- 1879-2642. ; 1788:9, s. 1916-1923
- Related links:
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https://doi.org/10.1...
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http://dx.doi.org/10...
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https://urn.kb.se/re...
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https://lup.lub.lu.s...
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Abstract
Subject headings
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- The effects of varying the cationic sequence of oligotryptophan-tagged antimicrobial peptides were investigated in terms of peptide adsorption to model lipid membranes, liposome leakage induction, and antibacterial potency. Heptamers of lysine (K7) and arginine (R7) were lytic against Escherichia coli bacteria at low ionic strength. In parallel, both peptides adsorbed on to bilayers formed by E. coli phospholipids, and caused leakage in the corresponding liposomes. K7 was the more potent of the two peptides in causing liposome leakage, although the adsorption of this peptide on E. coli membranes was lower than that of R7. The bactericidal effect, liposome lysis, and membrane adsorption were all substantially reduced at physiological ionic strength. When a tryptophan pentamer tag was linked to the C-terminal end of these peptides, substantial peptide adsorption, membrane lysis, and bacterial killing was observed also at high ionic strength, and also for a peptide of lower cationic charge density (KNKGKKN-W5). Strikingly, the order of membrane lytic potential of the cationic peptides investigated was reversed when tagged. This and other aspects of peptide behavior and adsorption, in conjunction with effects on liposomes and bacteria, suggest that tagged and untagged peptides act by different lytic mechanisms, which to some extent counterbalance each other. Thus, while the untagged peptides act by generating negative curvature strain in the phospholipid membrane, the tagged peptides cause positive curvature strain. The tagged heptamer of arginine, R7W5, was the best candidate for E. coli membrane lysis at physiological salt conditions and proved to be an efficient antibacterial agent.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Farmaceutiska vetenskaper (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Pharmaceutical Sciences (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Klinisk medicin -- Dermatologi och venereologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Clinical Medicine -- Dermatology and Venereal Diseases (hsv//eng)
Keyword
- antimicrobial
- peptide
- adsorption
- oligotryptophan
- oligolysine
- oligoarginine
- membrane
- liposomes
- phospholipid
- bilayer
- PHARMACY
- FARMACI
- Pharmaceutical Physical Chemistry
- Farmaceutisk fysikalisk kemi
- Oligoarginine
- Oligolysine
- Oligotryptophan
- Ellipsometry
- Bacteria
- Liposome
- Membrane
- Bilayer
- Phospholipid
- End-tagged
- Peptide
- AMP
- Antimicrobial
Publication and Content Type
- ref (subject category)
- art (subject category)
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