74536-29-1Relevant articles and documents
PYRROLOBENZODIAZEPINE DIMER PRECURSOR AND LIGAND-LINKER CONJUGATE COMPOUND THEREOF
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Paragraph 0251; 0255, (2020/02/18)
The present invention relates to a pyrrolobenzodiazepine dimer prodrug and a ligand-linker conjugate compound thereof, a composition containing these, and therapeutic use thereof particularly as an anticancer drug. The stability of the compounds themselves and the stability thereof in plasma are excellent and the compounds are advantageous in terms of manifestation of toxicity, and thus the compounds are industrially useful in that it is possible to target proliferative diseases such as cancer, to perform a specific treatment, to maximize the drug efficacy, and to minimize the occurrence of side effects.
A new approach to the neoglycopeptides: Synthesis of urea- and carbamate-tethered N-acetyl-D-glucosamine amino acid conjugates
Ichikawa, Yoshiyasu,Ohara, Fumiyo,Kotsuki, Hiyoshizo,Nakano, Keiji
, p. 5009 - 5012 (2007/10/03)
(Chemical Equation Presented) A novel approach to the synthesis of Fmoc-protected neoglycopeptide building blocks is described. Oxidation of N-acetyl-D-glucosamine isonitrile afforded the corresponding highly reactive glycopyranosyl isocyanate, which reacted with amino acid derivatives to furnish the corresponding urea- and carbamate-tethered Fmoc-protected N-acetyl-D-glucosamine amino acid conjugates in good yields.
Utilization of alternate substrates by the first three modules of the epothilone synthetase assembly line
Schneider, Tanya L.,Walsh, Christopher T.,O'Connor, Sarah E.
, p. 11272 - 11273 (2007/10/03)
The epothilones, a family of macrolactone natural products produced by the myxobacterial species Sorangium cellulosum, are of current clinical interest as antitumor agents. Inspection of the structure of the epothilones suggests a hybrid polyketide/nonribosomal peptide biosynthetic origin, and the recent sequencing of the epothilone biosynthetic gene cluster has validated this proposal. Here we have examined unnatural substrates with the first two enzymes of the biosynthetic pathway, EpoA and EpoB, to investigate the enzymatic construction of alternate heterocyclic structures and the subsequent elongation of these products by the third enzyme of the pathway, EpoC. The epothilone biosynthetic machinery can utilize serine to install an oxazole in place of a thiazole in the epothilone structure and will tolerate functionalized donor groups from the EpoA-ACP domain to produce epothilone fragments modified at the C21 position. These studies with the early enzymes of the epothilone biosynthesis cluster suggest that combinatorial biosynthesis may be a viable means for producing a variety of epothilone analogues that incorporate diversity into the heterocycle starter unit. Copyright
Synthesis of alanine and proline amino acids with amino or guanidinium substitution on the side chain
Zhang, Zhenyu,Aerschot, Arthur Van,Hendrix, Chris,Busson, Roger,David, Frank,Sandra, Pat,Herdewijn, Piet
, p. 2513 - 2522 (2007/10/03)
Competitive binding of peptides containing basic amino acids to disrupt or prevent the Tat-TAR interaction could result in diminished transcription as well as translation and hence constitutes an alternative way of controlling HIV replication. Therefore, we synthesized guanidinium and amino containing amino acids, based on a proline or an alanine scaffold. The introduction of the guanidinium moiety was best accomplished using 1H- pyrazole-1-carboxamidine hydrochloride, with Pmc used for its protection. The absence of racemization, maintained throughout the whole synthesis, was confirmed by chiral purity determination. These building blocks were smoothly incorporated into oligopeptides, which proved their suitability for use in a combinatorial approach for selecting TAR binding ligands. (C) 2000 Elsevier Science Ltd.
Tripeptide aldehyde inhibitors of human rhinovirus 3C protease: Design, synthesis, biological evaluation, and cocrystal structure solution of P1 glutamine isosteric replacements
Webber, Stephen E.,Okano, Koji,Little, Thomas L.,Reich, Siegfried H.,Xin, Yue,Fuhrman, Sheila A.,Matthews, David A.,Love, Robert A.,Hendrickson, Thomas F.,Patick, Amy K.,Meador III, James W.,Ferre, Rose Ann,Brown, Edward L.,Ford, Clifford E.,Binford, Susan L.,Worland, Stephen T.
, p. 2786 - 2805 (2007/10/03)
The investigation of tripeptide aldehydes as reversible covalent inhibitors of human rhinovirus (HRV) 3C protease (3CP) is reported. Molecular models based on the apo crystal structure of HRV-14 3CP and other trypsin- like serine proteases were constructe
Synthesis and opioid activity of conformationally constrained dynorphin A analogues. 1. Conformational constraint in the 'message' sequence
Arttamangkul,Murray,DeLander,Aldrich
, p. 2410 - 2417 (2007/10/02)
A constrained analogue of the opioid peptide dynorphin A (Dyn A) cyclized in the 'message' sequence was designed which may be compatible with the helical conformation proposed by Schwyzer (Biochemistry 1986, 25, 4281-4286) as the conformation Dyn A adopts
Total synthesis and absolute stereochemistry of the antifungal dipeptide Sch 37137 and its 2S,3S-isomer
Rane, Dinanath F.,Girijavallabhan, Viyyoor M.,Ganguly, Ashit K.,Pike, Russell E.,Saksena, Anil K.,McPhail, Andrew T.
, p. 3201 - 3204 (2007/10/02)
The absolute stereochemistry of the epoxide moiety in Sch 37137 has been established as 2R, 3R by its synthesis from L-tartaric acid.