Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/177670
Title: Lysine Scanning of Arg10-Teixobactin. Deciphering the Role of Hydrophobic and Hydrophilic Residues.
Author: Monaim, Shimaa A.H. Abdel
Jad, Yahya E.
Ramchuran, Estelle J.
El Faham, Ayman
Govender, Thavendran
Kruger, Hendrik G.
de la Torre, Beatriz G.
Albericio Palomera, Fernando
Keywords: Agents antiinfecciosos
Anàlisi d'aminoàcids
Anti-infective agents
Amino acids analysis
Issue Date: 31-Dec-2016
Publisher: American Chemical Society
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.
Note: Reproducció del document publicat a: https://doi.org/10.1021/acsomega.6b00354
It is part of: ACS Omega , 2016, vol. 1, num. 6, p. 1262-1265
URI: http://hdl.handle.net/2445/177670
Related resource: https://doi.org/10.1021/acsomega.6b00354
ISSN: 2470-1343
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)

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