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Synthesis and Biological Activity of Transmembrane Peptides Derived from FPR Family Receptors

  • Daisuke Sugiyama
  • Ryo Hayashi
  • Satoshi Osada
  • Yuhei Hamasaki
  • Ichiro Fujita
  • Hiroaki Kodama
Part of the Advances in Experimental Medicine and Biology book series (volume 611)

Introduction

Receptors, translocators and membrane enzymes exist as membrane integral proteins upon cellular surface. They are known to function as dimers or even higher oligomers. It is reported that transmembrane (TM) peptides derived from membrane integral protein modulated dimerization and consecutive function of parent proteins [1]. Neutrophils act as the first line of defense against the invasion of microorganisms in the body. Bacterial metabolites such as N-formylmethionyl peptides are chemoattractants for neutrophils and bind to specific surface receptors, N-formyl peptide receptor (FPR) that trigger specific host defensive processes such as chemotactic migration and killing of microorganisms through superoxide and phagocytosis. Human FPR was first defined biochemically in 1976, as a high-affinity binding site on the surface of neutrophils for prototypic N-formyl peptide, formyl-Met-Leu-Phe-OH (fMLP) [2]. FPR has the structure of seven membrane-spanning α-helical domains, and...

Keywords

Formyl Peptide Receptor Transmembrane Peptide Significant Blue Shift Specific Surface Receptor Short Peptide Fragment 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  • Daisuke Sugiyama
    • 1
  • Ryo Hayashi
    • 1
  • Satoshi Osada
    • 1
  • Yuhei Hamasaki
    • 2
  • Ichiro Fujita
    • 2
  • Hiroaki Kodama
    • 1
  1. 1.Department of Chemistry, Faculty of Science and EngineeringSaga UniversitySagaJapan
  2. 2.Department of Pediatrics, Faculty of MedicineSaga UniversitySagaJapan

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