Protease inhibitors from a water bloom of the cyanobacterium Microcystis aeruginosa

Autor:	Shmuel Carmeli, Vered Reshef
Rok vydání:	2001
Předmět:	Cyanobacteria Chromatography Protease biology Chemistry medicine.medical_treatment Organic Chemistry Absolute configuration biology.organism_classification Mass spectrometry Biochemistry High-performance liquid chromatography Microcystis Drug Discovery medicine Microcystis aeruginosa Microcin SF608
Zdroj:	Tetrahedron. 57:2885-2894
ISSN:	0040-4020
DOI:	10.1016/s0040-4020(01)00141-7
Popis:	Five new protease inhibitors, micropeptins SD944 ( 1 ), SD979 ( 2 ), SD999 ( 3 ) and SD1002 ( 4 ) and microginin SD755 ( 5 ) were isolated along with two known inhibitors, micropeptin SF995 ( 6 ) and microcin SF608 ( 7 ), from the hydrophilic extract of Microcystis aeruginosa . The planar structure of compounds 1 – 5 was determined by homonuclear and inverse-heteronuclear 2D-NMR techniques as well as high-resolution mass spectrometry. The absolute configuration of the asymmetric centers was studied using Marfey's method for HPLC. Compounds 1 – 4 , 6 and 7 are serine-protease inhibitors while compound 5 was found to inhibit amino-proteases.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::0c53ae7151e69d556ee1c88c6766966b https://doi.org/10.1016/s0040-4020(01)00141-7 Zobrazit plný text záznamu Full Text from ScienceDirect