128972-27-0Relevant articles and documents
Synthesis and Spectroscopic Properties of Fluorinated Coumarin Lysine Derivatives
Shukla, Lakshmi,Moodie, Lindon W. K.,Kindahl, Tomas,Hedberg, Christian
supporting information, p. 4792 - 4799 (2018/04/25)
The site-selective incorporation of fluorescent amino acids into proteins has emerged as a valuable alternative to expressible protein reporters. For successful application, a robust and scalable, yet flexible, route to non-natural amino acids is required. This work describes an improved synthesis of coumarin-conjugated lysine derivatives where fluorinated variants are accessed. These analogues can be utilized at low pH and should find application probing biological processes that operate under acidic conditions.
Convenient synthesis of Nε-(carboxymethyl)lysine, a key advanced glycation endproduct biomarker
Andersen, Jeanette M.,Hjelmgaard, Thomas,Dragsted, Lars O.,Nielsen, John
scheme or table, p. 531 - 534 (2012/04/04)
Advanced glycation endproducts (AGEs) are formed when sugars react with peptides and proteins without the help of enzymes and by thermal processing of food such as baking and frying. AGEs and especially N-(carboxymethyl) lysine (CML) has been used as general key biomarkers for oxidative stress and a number of diseases associated with poor lifestyle. Herein we present the first synthetic pathway to the free zwitter ion of CML via a protected intermediate. Georg Thieme Verlag Stuttgart · New York.
Synthesis and evaluation of peptidic maleimides as transglutaminase inhibitors
Halim, Dany,Caron, Karine,Keillor, Jeffrey W.
, p. 305 - 308 (2007/10/03)
A series of novel transglutaminase inhibitors was prepared, based on the scaffold of a commonly used peptide substrate and bearing an electrophilic maleimide group. These compounds were evaluated in vitro and shown to lead to irreversible inactivation of tissue transglutaminase. Comparison with inhibitors studied previously provides insight into the steric environment of the enzyme active site.
Solid-Phase Synthesis of DOTA-Peptides
De Leon-Rodriguez, Luis M.,Kovacs, Zoltan,Dieckmann, Gregg R.,Sherry, A. Dean
, p. 1149 - 1155 (2007/10/03)
A general synthetic route to two DOTA-linked N-Fmoc amino acids (DOTA-F and DOTA-K) is described that allows insertion of DOTA at any endo-position within a peptide sequence. Three model pentapeptides were prepared to test the general utility of these derivatives in solid-phase peptide synthesis. Both DOTA derivatives reacted smoothly by means of standard HBTU activation chemistry to the point of insertion of the DOTA amino acid, but extension of the peptide chain beyond the DOTA-amino acid insertion required the use of pre-activated C-pentafluorophenyl ester N-α-Fmoc amino acids. Three Gal-80 binding peptides (12-mers) were then prepared by using this methodology with DOTA positioned either at the N terminus or at one of two different internal positions;the binding of the resulting GdDOTA-12-mers to Gal-80 were compared. The methodology described here allows versatile, controlled introduction of DOTA into any location within a peptide sequence. This provides a potential method for the screening of libraries of DOTA-linked peptides for optimal targeting properties.
1,2,4-Triazolopyrazine Derivatives with Human Renin Inhibitory Activity. 1. Synthesis and Biological Properties of Alkyl Alcohol and Statine Derivatives
Roberts, David A.,Bradbury, Robert H.,Brown, David,Faull, Alan,Griffiths, David,et al.
, p. 2326 - 2334 (2007/10/02)
A series of 1,2,4-triazolopyrazine derivatives with human renin inhibitory activity, which incorporate (1S,2S)-2-amino-1,3-dicyclohexyl-1-hydroxypropane, statine (Sta), and (3S,4S)-4-amino-5-cyclohexyl-3-hydroxypentanoic acid (ACHPA) transition-state mimetics, have been prepared.Structure-activity relationships for renin inhibitory activity in the series are consistent with the 2-pyrazin-3-yl>-3-(3-pyridyl)propionic acid moiety 10b acting as a non-peptidic replacement for the P4-P2 (Pro-Phe-His) residues of the natural substrate angiotensinogen.Compounds 12m, 12o, and 12q were potent inhibitors of partially purified human renin (IC50 values 1.7, 6.8, and 3.7 nM, respectively), and also effectively lowered blood pressure in anesthetized, sodium depleted marmosets following intravenous administration.On oral administration however, no blood pressure lowering activity could be detected, and absorption studies in bile duct cannulated rats indicate that this may be due primarily to poor oral absorption, rather than rapid biliary excretion.The reason for the observed poor oral activity is not clear, but it seems unlikely that poor aqueous solubility or metabolic instability to gut enzymes are rate-determining, and other factors such as high molecular weight may also be very important.
