59524-71-9Relevant academic research and scientific papers
Inhibitors for bacterial cell-wall recycling
Yamaguchi, Takao,Blazquez, Blas,Hesek, Dusan,Lee, Mijoon,Llarrull, Leticia I.,Boggess, Bill,Oliver, Allen G.,Fisher, Jed F.,Mobashery, Shahriar
, p. 238 - 242 (2012/05/04)
Gram-negative bacteria have evolved an elaborate process for the recycling of their cell wall, which is initiated in the periplasmic space by the action of lytic transglycosylases. The product of this reaction, β-d-N- acetylglucosamine-(1a?'4)-1,6-anhydro-β-d-N-acetylmuramyl-l- Ala-I-d-Glu-meso-DAP-d-Ala-d-Ala (compound 1), is internalized to begin the recycling events within the cytoplasm. The first step in the cytoplasmic recycling is catalyzed by the NagZ glycosylase, which cleaves in a hydrolytic reaction the N-acetylglucosamine glycosidic bond of metabolite 1. The reactions catalyzed by both the lytic glycosylases and NagZ are believed to involve oxocarbenium transition species. We describe herein the synthesis and evaluation of four iminosaccharides as possible mimetics of the oxocarbenium species, and we disclose one as a potent (compound 3, Ki = 300 A± 15 nM) competitive inhibitor of NagZ.
Synthesis of two possible disulfide bonds containing peptide fragments (Cys6-Cys47, Cys48-Cys52 (Type I), and Cys6-Cys48, Cys47-Cys52 (Type II) of H-IGF-I) for the identification of disulfide bond linkage in recombinantly produced H-IGF-I
Iwai, Michio,Yamada, Hisashi,Ishii, Yoshinori,Tamura, Kouichi,Niwa, Mineo,Kobayashi, Masakazu
, p. 1827 - 1835 (2007/10/03)
The primary structure of human IGF-I, except for the disulfide bond system, has been reported by Rinderknecht and Humbel. IGF-I afforded the corresponding characteristic peptide fragments on V8 protease digestion, which contained Cys6, Cys47, Cys48, and Cys52. Two possible fragments, Type I with Cys6-Cys47 and Cys48-Cys52 and Type II with Cys6-Cys48 and Cys47-Cys52 of h-IGF-I(4-9,47-53), were chemically synthesized. The disulfide bond system of IGF-I was unequivocally determined to be the Type-II form along with Cys18-Cys61. Interestingly, the Type-I system was included in the disulfide bond isomer produced as the main by-product in the refolding step on IGF-I synthesis by the recombinant DNA method.
Peptide Synthesis in Aqueous Solution. V. Properties and Reactivities of (p-Hydroxyphenyl)benzylmethylsulfonium Salts for Direct Benzyl Esterification of N-Acylpeptides
Nakata, Takashi,Nakatani, Masaru,Takahashi, Masatoshi,Okai, Jiro,Kawaoka, Yoshiaki,Kouge, Katsushige,Okai, Hideo
, p. 1099 - 1106 (2007/10/03)
Some (p-hydroxyphenyl)benzylmethylsulfonium salts were prepared. These compounds generated a benzyl cation and converted not only N-acylamino acids but also N-acylpeptides into their corresponding benzyl esters without causing the racemization.
A Proton N.M.R. Study of the Conformation of Trp-Gly-Ala-Glu in Dimethyl Sulfoxide and Water
Beilharz, Georg R.,Fong, Joyce,Mack, Philip O. L.,Robertson, Alexander V.,Wright, Peter E.
, p. 751 - 758 (2007/10/02)
Proton nuclear magnetic resonance parameters are reported for Trp-Gly-Ala-Glu, constituting residues 115-118 of bovine myelin basic protein, in dimethyl sulfoxide solution.The 3JNH,α vicinal coupling constants which were used to dete
