122818-32-0Relevant academic research and scientific papers
Synthesis and evaluation of chloromethyl sulfoxides as a new class of selective irreversible cysteine protease inhibitors
Brouwer, Arwin J.,Bunschoten, Anton,Liskamp, Rob M.J.
, p. 6985 - 6993 (2008/03/28)
The synthesis and biological evaluation of a new class of selective irreversible cysteine protease inhibitors is described. A set of amino acid based chloromethyl sulfoxides was prepared and they were found to inhibit irreversibly the cysteine protease papain. They were selective for cysteine proteases since no inhibition was found for the serine protease chymotrypsin.
Synthesis of Peptidosulfinamides and Peptidosulfonamides: Peptidomimetics Containing the Sulfinamide or Sulfonamide Transition-State Isostere
Moree, Wilna J.,Marel, Gijs A. van der,Liskamp, Rob J.
, p. 5157 - 5169 (2007/10/02)
Synthetic routes are described toward the preparation of α- as well as β-substituted aminoethanesulfinyl chlorides, starting from either an aldehyde or from an amino acid derivative.The sulfinyl chlorides are used as building blocks for the preparation of homochiral α- or β-substituted sulfinamide and sulfonamide transition-state isosteres.The methodology has been applied to the synthesis of peptidosulfonamide peptidomimetics such as a hapten needed for the generation of antibodies and potential HIV protease inhibitors.In addition, the β-substituted aminoethanesulfinyl chlorides were used as building blocks for the preparation of a tetrapeptidosulfonamide, which can be considered as a biopolymer mimetic, employing a repetition of a cycle of three reactions: coupling of the sulfinyl chloride to the N-terminus of the growing peptidosulfonamide, oxidation to the sulfonamide, and deprotection of the N-terminus.
Potent and systemically active aminopeptidase N inhibitors designed from active-site investigation
Fournie-Zaluski,Coric,Turcaud,Bruetschy,Lucas,Noble,Roques
, p. 1259 - 1266 (2007/10/02)
Derivatives of amino acids bearing various zinc-coordinating moieties (SH, COOH, CONHOH, and PO3H2) were synthesized and tested for their ability to inhibit aminopeptidase N (APN). Among them, β-amino thiols were found to be the most
Synthesis of peptides containing the β-substituted aminoethane sulfinamide or sulfonamide transition-state isostere derived from amino acids
Moree, Wilna J.,Van Der Marel, Gijs A.,Liskamp Rob
, p. 6389 - 6392 (2007/10/02)
α-amino acids can be converted to homochiral β-substituted aminoethane sulfinamide or sulfonamide transition-state isosteres, which can be incorporated into peptides. These transition-state analogues e.g. the sulfonamide isostere of Phe-Phe will be used for the generation of catalytic antibodies as well as for the development of protease inhibitors.
The role of hydroxymethyl function on the biological activity of the antitumor antibiotic sparsomycin
Van den Broek,Fennis,Arevalo,Lazaro,Ballesta,Lelieveld,Ottenheijm
, p. 503 - 510 (2007/10/02)
The synthesis is described of the sparsomycin analogues 11-14 from the L-amino acids valine, isoleucine, phenylalanine and proline, respectively. The sparsomycin derivative 21 was not prepared in a similar way from glycine, but from cystamine following a different reaction route. These analogues, as well as the O-methylated and O-acetylated derivatives 15 and 16, respectively, were tested in vitro for their protein synthesis inhibitory activity and for their inhibition of colony formation of murine leukemia L1210 cells. The results of these assays indicate that the hydroxymethyl function of 1 is not essential for its biological activity, and that increase of lipophilicity in this 'northern' region of 1 does not noticeably affect the activity of the drug.
