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Lysine Scanning of Arg₁₀-Teixobactin: Deciphering the Role of Hydrophobic and Hydrophilic Residues.

ABSTRACT: Teixobactin is a recently discovered antimicrobial cyclodepsipeptide with good activity against Gram positive bacteria. Taking Arg₁₀-teixobactin as a reference, where the nonproteinogenic residue l-allo-enduracididine was substituted by arginine, a lysine scan was performed to identify the importance of keeping the balance between hydrophilic and hydrophobic amino acids for the antimicrobial activities of this peptide family. Thus, the substitution of four isoleucine residues present in the natural sequence by lysine led to a total loss of activity. On the other hand, the substitution of the polar noncharged residues and alanine by lysine allowed us to keep and in some cases to improve the antimicrobial activity.

SUBMITTER: Abdel Monaim SAH

PROVIDER: S-EPMC6044708 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

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Lysine Scanning of Arg10-Teixobactin: Deciphering the Role of Hydrophobic and Hydrophilic Residues.

Abdel Monaim Shimaa A H SAH Jad Yahya E YE Ramchuran Estelle J EJ El-Faham Ayman A Govender Thavendran T Kruger Hendrik G HG de la Torre Beatriz G BG Albericio Fernando F

ACS omega 20161219 6

Teixobactin is a recently discovered antimicrobial cyclodepsipeptide with good activity against Gram positive bacteria. Taking Arg10-teixobactin as a reference, where the nonproteinogenic residue l-allo-enduracididine was substituted by arginine, a lysine scan was performed to identify the importance of keeping the balance between hydrophilic and hydrophobic amino acids for the antimicrobial activities of this peptide family. Thus, the substitution of four isoleucine residues present ...[more]

PMID: 30023506

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