کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1391788 | 983641 | 2006 | 9 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Engineering Dehydro Amino Acids and Thioethers into Peptides Using Lacticin 481 Synthetase Engineering Dehydro Amino Acids and Thioethers into Peptides Using Lacticin 481 Synthetase](/preview/png/1391788.png)
SummaryLantibiotics are peptide antimicrobials containing the thioether-bridged amino acids lanthionine (Lan) and methyllanthionine (MeLan) and often the dehydrated residues dehydroalanine (Dha) and dehydrobutyrine (Dhb). While biologically advantageous, the incorporation of these residues into peptides is synthetically daunting, and their production in vivo is limited to peptides containing proteinogenic amino acids. The lacticin 481 synthetase LctM offers versatile control over the installation of dehydro amino acids and thioether rings into peptides. In vitro processing of semisynthetic substrates unrelated to the prelacticin 481 peptide demonstrated the broad substrate tolerance of LctM. Furthermore, a chemoenzymatic strategy was employed to generate novel thioether linkages by cyclization of peptidic substrates containing the nonproteinogenic cysteine analogs homocysteine and β-homocysteine. These findings are promising with respect to the utility of LctM toward preparation of conformationally constrained peptide therapeutics.
Journal: - Volume 13, Issue 10, October 2006, Pages 1109–1117