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Solution structure of the antimicrobial peptide gaegurin 4 by ^1^H and ^15^N nuclear magnetic resonance spectroscopy by Sang-Ho Park; Yun-Kyong Kim; Jung-Won Park; ByeongJae Lee; Bong-Jin Lee is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Gaegurin 4 (GGN4) is a 37‐residue antimicrobial peptide isolated from the skin of a Korean frog, __Rana rugosa__. This peptide shows a broad range of activity against prokaryotic cells but shows very little hemolytic activity against human red blood cells. The solution structure of GGN4 was studied by using circular dichroism (CD) and NMR spectroscopy. CD investigations revealed that GGN4 adopts mainly an α‐helical conformation in trifluoroethanol/water solution, in dodecylphosphocholine and in SDS micelles, but adopts random structure in aqueous solution. By using both homonuclear and heteronuclear NMR experiments, complete ^1^H and ^15^N resonance assignments were obtained for GGN4 in 50% trifluoroethanol/water solution. The calculated structures of GGN4 consist of two amphipathic α‐helices extending from residues 2–10 and from residues 16–32. These two helices are connected by a flexible loop spanning between the residues 11 and 15. By using enzyme digestion and matrix‐assisted laser desorption/ionization mass spectroscopy, we confirmed that GGN4 contains a disulfide bridge formed between the residues Cys31 and Cys37 in its C‐terminus. The effect of disulfide bridge on the struc

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Author

Sang-Ho Park; Yun-Kyong Kim; Jung-Won Park; ByeongJae Lee; Bong-Jin Lee

Publisher

John Wiley and Sons; Springer; Wiley (Blackwell Publishing); Springer-Verlag; Blackwell Publishing Inc.; Springer Verlag; Wiley; Springer Science and Business Media LLC (ISSN 1432-1327)

Published

2000

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)