Role of C-terminal heptapeptide in pore-forming activity of antimicrobial agent, gaegurin 4

The Journal of Peptide Research : Official Journal of the American Peptide Society
H J KimP D Ryu

Abstract

Gaegurin 4 (GGN4) is an antimicrobial peptide of 37 amino acids isolated from the skin of a frog, Rana rugosa. GGN4 has a disulfide bond between the residues 31 and 37, which is highly conserved among the antimicrobial peptides isolated from skin of the genus, Rana. However, the role of this C-terminal heptapeptide motif is not well understood. In this work, we compared the membrane effects of the full-length GGN4 (C37) and GGN4 1-30 (C30), which is devoid of the C-terminal seven amino acids to elucidate the function of the C-terminal motif. C37 induced significantly larger membrane conductance (>10x) in the model lipid bilayers formed with acidic and neutral phospholipids and larger K+ efflux from gram-positive (>30x) and gram-negative bacteria. However, the pores induced by C37 and C30 were not different in their permeability to K+ over Cl- (permeability ratio of K+ to Cl- = 4.8-7.1). In addition, the pore-forming effect of C37 or C30 in acidic membranes was not different from that in neutral membranes. Furthermore, C37-induced K+ efflux was not significantly decreased by the reducing agent, dithiothreitol. The results indicate that C-terminal heptapeptide sequence plays an important role in maintaining the high pore-forming ...Continue Reading

Citations

Dec 5, 2006·Biochemical and Biophysical Research Communications·Seung-Wook ChiKyou-Hoon Han
Mar 11, 2009·Biochimica Et Biophysica Acta·Evan F HaneyHans J Vogel
Dec 9, 2008·Biochimica Et Biophysica Acta·Hyung-Sik WonBong-Jin Lee
Nov 4, 2009·The Korean Journal of Physiology & Pharmacology : Official Journal of the Korean Physiological Society and the Korean Society of Pharmacology·Heejeong KimPan Dong Ryu
Jun 3, 2006·Natural Product Reports·Tara L PukalaMichael J Tyler
Feb 2, 2021·Chemical Reviews·Jasmin PortelinhaAlfredo M Angeles-Boza
Dec 4, 2019·Biochimica Et Biophysica Acta. Biomembranes·Erum MalikSarah R Dennison

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