RESUMO
Hirudin, a potent clinical thrombin inhibitor from Hirudo medicinalis, consists of 65 amino acids in a single chain. In this paper, we systematically synthesize a series of C-terminal (desulfo hirudin45-65) peptides substituted by 20 natural L-amino acids via the Multipin method. The resulting peptide library is subsequently screened using an alpha-thrombin-mediated fibrinogen clotting assay and alpha-thrombin-induced amidolytic hydrolysis assay.
Assuntos
Hirudinas/química , Amidas/metabolismo , Sequência de Aminoácidos , Sítios de Ligação , Bioensaio , Domínio Catalítico , Técnicas de Química Combinatória , Fibrinólise/efeitos dos fármacos , Hirudinas/metabolismo , Hirudinas/farmacologia , Hidrólise , Dados de Sequência Molecular , Biblioteca de PeptídeosRESUMO
Carbonyl chlorides substituted with aromatic dense-ring are chemically active and their fluorescent quantum yields are usually high and they may be used as fluorescent probes for detection of many compounds. Studies on their synthesis and structure activity relationship are very important in the micro-or supermicro-detection of drugs and toxicants containing hydroxy groups. Therefore, the probes may find wide application in the chemical engineering and pharmaceutical industry. Three new fluorescent probes: Beta-(9-anthracene) acrylonyl chloride, Beta-(9-anthracene) propionyl chloride and Beta-( 1-pyrene ) acrylonyl chloride were synthesized by the reaction between the corresponding acid and thionyl chloride. 1-Prenecarboxaldehyde synthesized by using pyrene and N-formyl-N-methylaniline with phosphorus oxychloride as catalyst, was allowed to react with malonic acid to produce Beta-(1-pyrene) acrylic acid for the last-mentioned acid chloride.
