In Silico Identification and Biological Evaluation of Antimicrobial Peptides Based on Human Cathelicidin LL-37

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Sigurdardottir, ThorgerdurLund University,Lunds universitet,Anestesiologi och intensivvård,Sektion II,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Anesthesiology and Intensive Care,Section II,Department of Clinical Sciences, Lund,Faculty of Medicine (author)

In Silico Identification and Biological Evaluation of Antimicrobial Peptides Based on Human Cathelicidin LL-37

Article/chapterEnglish2006

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2006
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LIBRIS-ID:oai:DiVA.org:uu-81955
https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-81955URI
https://doi.org/10.1128/AAC.01583-05DOI
https://lup.lub.lu.se/record/161378URI

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Language:English
Summary in:English

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Subject category:art swepub-publicationtype

Notes

Bacterial lipopolysaccharides (LPS) are important triggers of the widespread inflammatory response, which contributes to the development of multiple organ failure during sepsis. The helical 37-amino-acid-long human antimicrobial peptide LL-37 not only possesses a broad-spectrum antimicrobial activity but also binds and neutralizes LPS. However, the use of LL-37 in sepsis treatment is hampered by the fact that it is also cytotoxic. To find a less toxic analog of LL-37, we used in silico analysis to identify amphipathic helical regions of LL-37. A 21-amino-acid fragment (GKE) was synthesized, the biological actions of which were compared to those of two equally long peptides derived from the N and C termini of LL-37 as well as native LL-37. GKE displayed antimicrobial activity against Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, Candida albicans, and Candida parapsilosis that was similar to or even stronger than LL-37. GKE, as well as the equally long control peptides, attracted granulocytes in a fashion similar to that of LL-37, while only GKE was as potent as LL-37 in inhibiting LPS-induced vascular nitric oxide production. GKE caused less hemolysis and apoptosis in human cultured smooth muscle cells than LL-37. In summary, we have identified an active domain of LL-37, GKE, which displays antimicrobial activity in vitro and LPS-binding activity similar to those of LL-37 but is less toxic. GKE therefore holds promise as a template for the development of peptide antibiotics for the treatment of sepsis.

Subject headings and genre

MEDICIN OCH HÄLSOVETENSKAP Klinisk medicin Anestesi och intensivvård hsv//swe
MEDICAL AND HEALTH SCIENCES Clinical Medicine Anesthesiology and Intensive Care hsv//eng
MEDICIN OCH HÄLSOVETENSKAP Klinisk medicin Dermatologi och venereologi hsv//swe
MEDICAL AND HEALTH SCIENCES Clinical Medicine Dermatology and Venereal Diseases hsv//eng
MEDICINE
MEDICIN

Added entries (persons, corporate bodies, meetings, titles ...)

Andersson, PiaLund University (author)
Davoudi, MinaLund 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(Swepub:lu)derm-mda (author)
Malmsten, MartinUppsala University,Uppsala universitet,Institutionen för farmaci(Swepub:lu)ma1014ma (author)
Schmidtchen, ArturLund 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(Swepub:lu)derm-asc (author)
Bodelsson, MikaelLund University,Lunds universitet,Anestesiologi och intensivvård,Sektion II,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Anesthesiology and Intensive Care,Section II,Department of Clinical Sciences, Lund,Faculty of Medicine(Swepub:lu)anes-mbo (author)
Anestesiologi och intensivvårdSektion II (creator_code:org_t)

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In:Antimicrobial Agents and Chemotherapy50:9, s. 2983-29890066-48041098-6596

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