30189-51-6Relevant articles and documents
Enhancement of the small intestinal uptake of phenylalanylglycine via a H+/oligopeptide transport system by chemical modification with fatty acids
Fujita, Takuya,Morishita, Yutaka,Ito, Hitomi,Kuribayashi, Daisuke,Yamamoto, Akira,Muranishi, Shozo
, p. 2455 - 2465 (1997)
The transport characteristics of chemically modified phenylalanylglycine (PheGly) with butyric acid (C4-Phe-Gly) and caproic acid (C6-Phe-Gly) were examined using rabbit intestinal brush-border membrane vesicles (BBMVs). In the prese
Synthesis of fully Protected Peptides on a Tetraethyleneglycol Diacrylate (TTEGDA)-Crosslinked Polystyrene support with a Photolytically Detachable 2-Nitrobenzyl Anchoring group
Renil, M.,Pillai, V. N. Rajasekharan
, p. 3809 - 3812 (1994)
1-Chloromethyl-2-nitro tetraethyleneglycol diacrylate (TTEGDA)-crosslinked polystyrene resin was prepared by nitration of chloromethyl (4percent) TTEGDA-crosslinked polystyrene resin and used as a photosensitive solid support for the preparation of fully
Synthesis and conformational characterization of diketopiperazines bearing a benzyl moiety
Nakao, Michiyasu,Toriuchi, Yuriko,Fukayama, Shintaro,Sano, Shigeki
, p. 340 - 342 (2014/03/21)
Diketopiperazines bearing a benzyl moiety with different para-substituents were synthesized and analyzed by 1HNMR spectroscopy. All of these diketopiperazines were found to adopt a folded conformation according to the upfield chemical shift of the cis-proton (cis to the benzyl moiety) due to a shielding effect in the 1HNMR spectra. An intramolecular CH-π interaction appears to be an important factor for the folded conformation due to the effects of para-substituents on the benzyl group.
HMDO-promoted peptide and protein synthesis in ionic liquids
Duan, Jianli,Sun, Yao,Chen, Hao,Qiu, Guofu,Zhou, Haibing,Tang, Ting,Deng, Zixin,Hong, Xuechuan
, p. 7013 - 7022 (2013/08/23)
Hexamethyldisiloxane (HMDO) has been developed to efficiently promote the metal-free direct coupling of an amino function of one cysteine-free peptide or protein and a C-terminal thioester of the second peptide in ionic liquids. The amide-coupling reaction proceeds smoothly under mild conditions to afford the corresponding products in good to excellent yields (63-94%). Peptide couplings were also achieved using in-situ-generated thioesters by the thioesterification of oxo esters.