2026-04-13T02:18:10Zhttps://recercat.cat/oai/request

oai:recercat.cat:2445/1776702025-12-04T21:40:58Zcom_2072_1057col_2072_478917col_2072_478933

00925njm 22002777a 4500 dc Monaim, Shimaa A.H. Abdel author Jad, Yahya E. author Ramchuran, Estelle J. author El Faham, Ayman author Govender, Thavendran author Kruger, Hendrik G. author de la Torre, Beatriz G. author Albericio Palomera, Fernando author 2021-05-27T10:02:52Z 2021-05-27T10:02:52Z 2016-12-31 2021-05-27T10:02:52Z 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. Agents antiinfecciosos Anàlisi d'aminoàcids Anti-infective agents Amino acids analysis Lysine Scanning of Arg10-Teixobactin. Deciphering the Role of Hydrophobic and Hydrophilic Residues.