95015-69-3Relevant articles and documents
A simple and rapid protocol for N-methyl-α-amino acids
Reddy, G. Vidyasagar,Iyengar
, p. 299 - 300 (2007/10/03)
A two step strategy for optically pure N-Protected-N-methyl-α-amino acids starting from N-protected-α-amino acids via reductive cleavage of oxazolidinones using NaCNBH3/TMSCl is described.
Intestinal absorption of fluorescence-derivatized cationic peptide 001-C8-NBD via adsorptive-mediated transcytosis
Sai, Yoshimichi,Kajita, Masahiro,Tamai, Ikumi,Kamata, Makoto,Wakama, Jun,Wakamiya, Tateaki,Tsuji, Akira
, p. 841 - 848 (2007/10/03)
The intestinal absorption of an intact oligopeptide was investigated in rats using a synthetic cationic peptide, 001-C8 (H-MeTyr-Arg-MeArg-d-Leu-NH(CH2)8NH2). The peptide was coupled with 4-nitrobenzo-2-oxa-1,3-diazole (NBD) to prepare a fluorescence-labeled derivative 001-C8-NBD (H-MeTyr-Arg-MeArg-d-Leu-NH(CH2)8NH-NBD) for the purpose of quantification. The degradation half-life of 001-C8-NBD in jejunal homogenate (1mg/mL) was 99.5min, which was significantly longer than that of natural leucine enkephalin (1.14min). The absorption of 001-C8-NBD was evaluated by the vascular-perfusion method. Intact 001-C8-NBD appeared in the blood time-dependently and the absorption volume at 30min (2.75 ± 0.14μL/cm intestine) was significantly larger than that of [3H]PEG 900 (0.88 ± 0.13μL/cm intestine), of which membrane permeability is very low. The absorption of 001-C8-NBD was greatly reduced by an adsorptive-mediated endocytosis inhibitor, protamine (10mM). No inhibition of the absorption of [3H]PEG 900 by protamine was observed. The intestinal absorption was also measured by an in vivo loop method. The absorption clearance of 001-C8-NBD measured by this method (0.083 ± 0.008μL/min/cm intestine) was comparable to that obtained by the vascular perfusion method (0.092 ± 0.005μL/min/cm intestine). All of these data suggested that 001-C8-NBD was absorbed as the intact oligopeptide in the intestine in vivo. Adsorptive-mediated transcytosis is suggested to have enormous potential as an oral delivery system for peptide and/or protein drugs. Copyright (C) 1998 Elsevier Science Ltd.
Analgesic dipeptide amides and method of use and compositions thereof
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, (2008/06/13)
A genus of dipeptide amides including as the preferred subgenus the dipeptide amides having the structural formula R1 TyrR2 D-AlaNHR4 wherein R1 and R2 are each hydrogen or alkyl provided that at least one of them is other than hydrogen and R4 is phenylalkyl or substituted-phenylalkyl are prepared by condensing the dipeptide with the amine or the amino acid with the amino acid amide and are useful as analgesics.