1139906-45-8Relevant academic research and scientific papers
Correct disulfide pairing is required for the biological activity of crustacean androgenic gland hormone (AGH): Synthetic studies of AGH
Katayama, Hidekazu,Hojo, Hironobu,Ohira, Tsuyoshi,Ishii, Akira,Nozaki, Takamichi,Goto, Kiyomi,Nakahara, Yuko,Takahashi, Tetsuo,Hasegawa, Yuriko,Nagasawa, Hiromichi,Nakahara, Yoshiaki
experimental part, p. 1798 - 1807 (2011/02/21)
Androgenic gland hormone (AGH) of the woodlouse, Armadillidium vulgare, is a heterodimeric glycopeptide. In this study, we synthesized AGH with a homogeneous N-linked glycan using the expressed protein ligation method. Unexpectedly, disulfide bridge arran
Synthesis and antibacterial activities of N-Glycosylated derivatives of tyrocidine a, a macrocyclic peptide antibiotic
Honggang, Hu,Jie, Xue,Swarts, Benjamin M.,Qianli, Wang,Qiuye, Wu,Zhongwu, Guo
experimental part, p. 2052 - 2059 (2009/12/30)
An efficient and practical method for macrocyclic glycopeptide synthesis was developed and utilized to synthesize tyrocidine A and its glycosylated derivatives. The method is based on solid-phase peptide synthesis using 2-chlorotrityl resin as the solid-phase support and glycosyl amino acids as building blocks. After glycopeptides with fully protected glycans and side chains were released from the acid-labile resin, their Cand N-termini were intramolecularly coupled in solution to afford cyclic glycopeptides in quantitative yields. This synthetic method should be generally applicable to various macrocyclic glycopeptides. Biological studies of the synthetic tyrocidine A derivatives showed that linking glycans directly to the Asn residue of tyrocidine A diminished its antibacterial activity, but linking glycans to Asn via a simple spacer did not. These results Revealed the important impact of glycans on the activities, and probably the structures, of glycopeptide antibiotics.
