5/12/2023 0 Comments Thiol functional groupAdama Mickiewicza W Poznaniu filed Critical Instytut Chemii Bioorganicznej Polskiej Akademii Nauk Publication of WO2013165266A1 publication Critical patent/WO2013165266A1/en Links Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.) Filing date Publication date Priority to P元99003A priority Critical patent/PL222577B1/en Priority to PLP.399003 priority Application filed by Instytut Chemii Bioorganicznej Polskiej Akademii Nauk, Fundacja Uniwersytetu Im. Adama Mickiewicza W Poznaniu Priority date (The priority date is an assumption and is not a legal conclusion. Inventor Wojciech Tadeusz MARKIEWICZ Marcin Krzysztof Chmielewski Sylwia Maria MUSIAŁ Hieronim Franciszek MACIEJEWSKI Grzegorz HRECZYCHO Original Assignee Instytut Chemii Bioorganicznej Polskiej Akademii Nauk Fundacja Uniwersytetu Im. Google Patents Method for protecting hydroxyl, amine or thiol functional groups with tetraisopropydisilane and the corresponding protected compoundsĭownload PDF Info Publication number WO2013165266A1 WO2013165266A1 PCT/PL2013/000058 PL2013000058W WO2013165266A1 WO 2013165266 A1 WO2013165266 A1 WO 2013165266A1 PL 2013000058 W PL2013000058 W PL 2013000058W WO 2013165266 A1 WO2013165266 A1 WO 2013165266A1 Authority WO WIPO (PCT) Prior art keywords amine group hydroxyl thiol carbon atoms Prior art date Application number PCT/PL2013/000058 Other languages French ( fr) Google Patents WO2013165266A1 - Method for protecting hydroxyl, amine or thiol functional groups with tetraisopropydisilane and the corresponding protected compounds All rights reserved.WO2013165266A1 - Method for protecting hydroxyl, amine or thiol functional groups with tetraisopropydisilane and the corresponding protected compounds Therefore, this study provides an excellent basis to develop promising antimicrobial agents that possess a broad range of antimicrobial activities with less susceptibility for development of drug resistance.Ĭopyright © 2011 Elsevier Ltd. In addition, the peptides are shown not to induce secretion of IFN-γ and TNF-α in human monocytes as compared to lipopolysaccharide, which implies additional safety aspects of the peptides to be used as both systemic and topical antimicrobial agents. However, the same treatment with conventional antibiotics penicillin G or ciprofloxacin easily develop resistance in the treated microbes. Multiple treatments of microbes with this peptide at sub MIC concentration do not induce resistance, even up to passage 10. Microscopy studies suggest that this peptide kills microbial cells by inducing pores of ∼20-30 nm in size in microbial membrane on a short time scale, which further develops to grossly damaged membrane envelope on a longer time scale. At the MIC levels, this peptide does not induce significant hemolysis, and its MIC values occur at the concentration of more than 10 times of their corresponding 50% hemolysis concentrations (HC(50)). In particular, the AMP with 2 cysteine residues at the terminal ends of the peptide and 2 repeat units of LLKK, i.e., C(LLKK)(2)C, has been demonstrated to have high selectivity towards a wide range of microbes from Gram-positive Bacillus subtilis, Gram-negative Escherichia coli, Pseudomonas aerogenosa, and yeast Candida albicans over red blood cells. A series of synthetic AMPs capable of forming α-helical structures and containing free-sulfhydryl groups are designed in this study ((LLKK)(2)C, C(LLKK)(2)C, (LLKK)(3)C, C(LLKK)(3)C). Antimicrobial peptides (AMP) have been proposed as blueprints for the development of new antimicrobial agents for the treatment of drug resistant infections.
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