Antimicrobial decapeptide KSL-W enhances neutrophil chemotaxis and function

Richard L. Williams, Herve Y. Sroussi, Kai Leung, Phillip Marucha

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Mammalian cationic antimicrobial peptides have received increased attention over the last decade, due to their prokaryotic selectivity and decreased risk of microbial resistance. In addition, antimicrobial peptides display differential biological effects on mammalian immune cell function, such as migration, adhesion, and modulation of respiratory burst, which make them even more attractive as therapeutic agents. Synthetic combinatorial libraries provide a time-efficient and cost-effective source for these diverse molecules. The novel synthetic antimicrobial peptide, KSLW (KKVVFWVKFK-NH 2), has been shown to display a broad spectrum of antimicrobial activity against Gram (+) and Gram (-) bacteria, fungi and viruses. In this study, we evaluated the alternative biological activity of the decapeptide on neutrophil migration and function. KSLW was demonstrated to be chemotactic for neutrophils in micromolar amounts, and neutrophil treatment with KSLW, after 1 min, resulted in significant increases in F-actin polymerization. KSLW was shown to inhibit oxygen radical production in PMA- and LPS-stimulated neutrophils. Future studies, to determine if KSLW regulates neutrophil phagocytosis, adhesion, and apoptosis, or examining the effect of KSLW on other mammalian cell types, such as cell populations of healing-impaired wounds, would provide significant insight for the potential therapeutic strategies offered by antimicrobial peptides.

Original languageEnglish (US)
Pages (from-to)1-8
Number of pages8
JournalPeptides
Volume33
Issue number1
DOIs
StatePublished - Jan 2012
Externally publishedYes

Fingerprint

Chemotaxis
Neutrophils
Peptides
Adhesion
Antimicrobial Cationic Peptides
Cells
Bioactivity
Fungi
Viruses
Actins
Reactive Oxygen Species
Bacteria
Polymerization
Modulation
Respiratory Burst
Apoptosis
Molecules
Phagocytosis
Wound Healing
Therapeutics

Keywords

  • Actin polymerization
  • Antimicrobial peptide
  • Chemotaxis
  • Multifunctional
  • Neutrophil

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Physiology
  • Cellular and Molecular Neuroscience

Cite this

Antimicrobial decapeptide KSL-W enhances neutrophil chemotaxis and function. / Williams, Richard L.; Sroussi, Herve Y.; Leung, Kai; Marucha, Phillip.

In: Peptides, Vol. 33, No. 1, 01.2012, p. 1-8.

Research output: Contribution to journalArticle

Williams, Richard L. ; Sroussi, Herve Y. ; Leung, Kai ; Marucha, Phillip. / Antimicrobial decapeptide KSL-W enhances neutrophil chemotaxis and function. In: Peptides. 2012 ; Vol. 33, No. 1. pp. 1-8.
@article{0b5c9310eb4145ef9efe955a0a9b2cb7,
title = "Antimicrobial decapeptide KSL-W enhances neutrophil chemotaxis and function",
abstract = "Mammalian cationic antimicrobial peptides have received increased attention over the last decade, due to their prokaryotic selectivity and decreased risk of microbial resistance. In addition, antimicrobial peptides display differential biological effects on mammalian immune cell function, such as migration, adhesion, and modulation of respiratory burst, which make them even more attractive as therapeutic agents. Synthetic combinatorial libraries provide a time-efficient and cost-effective source for these diverse molecules. The novel synthetic antimicrobial peptide, KSLW (KKVVFWVKFK-NH 2), has been shown to display a broad spectrum of antimicrobial activity against Gram (+) and Gram (-) bacteria, fungi and viruses. In this study, we evaluated the alternative biological activity of the decapeptide on neutrophil migration and function. KSLW was demonstrated to be chemotactic for neutrophils in micromolar amounts, and neutrophil treatment with KSLW, after 1 min, resulted in significant increases in F-actin polymerization. KSLW was shown to inhibit oxygen radical production in PMA- and LPS-stimulated neutrophils. Future studies, to determine if KSLW regulates neutrophil phagocytosis, adhesion, and apoptosis, or examining the effect of KSLW on other mammalian cell types, such as cell populations of healing-impaired wounds, would provide significant insight for the potential therapeutic strategies offered by antimicrobial peptides.",
keywords = "Actin polymerization, Antimicrobial peptide, Chemotaxis, Multifunctional, Neutrophil",
author = "Williams, {Richard L.} and Sroussi, {Herve Y.} and Kai Leung and Phillip Marucha",
year = "2012",
month = "1",
doi = "10.1016/j.peptides.2011.11.022",
language = "English (US)",
volume = "33",
pages = "1--8",
journal = "Peptides",
issn = "0196-9781",
publisher = "Elsevier Inc.",
number = "1",

}

TY - JOUR

T1 - Antimicrobial decapeptide KSL-W enhances neutrophil chemotaxis and function

AU - Williams, Richard L.

AU - Sroussi, Herve Y.

AU - Leung, Kai

AU - Marucha, Phillip

PY - 2012/1

Y1 - 2012/1

N2 - Mammalian cationic antimicrobial peptides have received increased attention over the last decade, due to their prokaryotic selectivity and decreased risk of microbial resistance. In addition, antimicrobial peptides display differential biological effects on mammalian immune cell function, such as migration, adhesion, and modulation of respiratory burst, which make them even more attractive as therapeutic agents. Synthetic combinatorial libraries provide a time-efficient and cost-effective source for these diverse molecules. The novel synthetic antimicrobial peptide, KSLW (KKVVFWVKFK-NH 2), has been shown to display a broad spectrum of antimicrobial activity against Gram (+) and Gram (-) bacteria, fungi and viruses. In this study, we evaluated the alternative biological activity of the decapeptide on neutrophil migration and function. KSLW was demonstrated to be chemotactic for neutrophils in micromolar amounts, and neutrophil treatment with KSLW, after 1 min, resulted in significant increases in F-actin polymerization. KSLW was shown to inhibit oxygen radical production in PMA- and LPS-stimulated neutrophils. Future studies, to determine if KSLW regulates neutrophil phagocytosis, adhesion, and apoptosis, or examining the effect of KSLW on other mammalian cell types, such as cell populations of healing-impaired wounds, would provide significant insight for the potential therapeutic strategies offered by antimicrobial peptides.

AB - Mammalian cationic antimicrobial peptides have received increased attention over the last decade, due to their prokaryotic selectivity and decreased risk of microbial resistance. In addition, antimicrobial peptides display differential biological effects on mammalian immune cell function, such as migration, adhesion, and modulation of respiratory burst, which make them even more attractive as therapeutic agents. Synthetic combinatorial libraries provide a time-efficient and cost-effective source for these diverse molecules. The novel synthetic antimicrobial peptide, KSLW (KKVVFWVKFK-NH 2), has been shown to display a broad spectrum of antimicrobial activity against Gram (+) and Gram (-) bacteria, fungi and viruses. In this study, we evaluated the alternative biological activity of the decapeptide on neutrophil migration and function. KSLW was demonstrated to be chemotactic for neutrophils in micromolar amounts, and neutrophil treatment with KSLW, after 1 min, resulted in significant increases in F-actin polymerization. KSLW was shown to inhibit oxygen radical production in PMA- and LPS-stimulated neutrophils. Future studies, to determine if KSLW regulates neutrophil phagocytosis, adhesion, and apoptosis, or examining the effect of KSLW on other mammalian cell types, such as cell populations of healing-impaired wounds, would provide significant insight for the potential therapeutic strategies offered by antimicrobial peptides.

KW - Actin polymerization

KW - Antimicrobial peptide

KW - Chemotaxis

KW - Multifunctional

KW - Neutrophil

UR - http://www.scopus.com/inward/record.url?scp=84855818323&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84855818323&partnerID=8YFLogxK

U2 - 10.1016/j.peptides.2011.11.022

DO - 10.1016/j.peptides.2011.11.022

M3 - Article

C2 - 22197491

AN - SCOPUS:84855818323

VL - 33

SP - 1

EP - 8

JO - Peptides

JF - Peptides

SN - 0196-9781

IS - 1

ER -