GLORIA — GEOMAR Library Ocean Research Information Access

Hits per page

hits 1 - 2 | 2 hits

Sorting

Electronic Resource

Novel heterocyclic inhibitors of matrix metalloproteinases: three 6H-1,3,4-thiadiazines (2001)

Schröder, Jörg ; Wenzel, Herbert ; Stammler, Hans Georg ; [et al.]

Oxford [u.a.] : International Union of Crystallography (IUCr)

Acta crystallographica 57 (2001), S. 593-596

add to mindlist on the mindlist

Details

ISSN: 1600-5759

Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001

Topics: Chemistry and Pharmacology , Geosciences , Physics

Notes: The title compounds, (2S)-N-[5-(4-chlorophenyl)-2,3-dihydro-6H-1,3,4-thiadiazin-2-ylidene]-2-[(phenylsulfonyl)amino]propanamide, C18H17ClN4O3S2, (I), (2R)-N-[5-(4-fluorophenyl)-6H-1,3,4-thiadiazin-2-yl]-2-[(phenylsulfonyl)amino]propanamide, C18H17FN4O3S2, (II), and (2S)-N-[5-(5-chloro-2-thienyl)-6H-1,3,4-thiadiazin-2-yl]-2-[(phenylsulfonyl)amino]propanamide, C16H15ClN4O3S3, (III), are potent inhibitors of matrix metalloproteinases. In all three compounds, the thiadiazine ring adopts a screw-boat conformation. The molecules of compound (I) show a short intramolecular NAla—H...Nexo hydrogen bond [N...N 2.661 (3) Å] and are linked into a chain along the c axis by Nendo—H...Sendo and Nendo—H...OAla hydrogen bonds [N...S 3.236 (3) and N...O 3.375 (3) Å] between neighbouring molecules. In compound (II), the molecules are connected antiparallel into a chain along the a axis by Nexo—H...OAla and NAla—H...Nendo hydrogen bonds [N...O 2.907 (6) and N...N 2.911 (6) Å]. The molecules of compound (III) are dimerized antiparallel through Nexo—H...Nendo hydrogen bonds [N...N 2.956 (7) and 2.983 (7) Å]. The different hydrogen-bonding patterns can be explained by an amido–imino tautomerism (prototropic shift) shown by different bond lengths within the 6H-1,3,4-thiadiazine moiety.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1107/S0108270101002372

Permalink

	Location	Call Number	Limitation	Availability

Others were also interested in ...

Paper (German National Licenses)

Fulltext

Electronic Resource

The Proteolytic Activity of the Recombinant Cryptic Human Fibronectin Type IV Collagenase from E. coli Expression (2000)

Schnepel, Jörn ; Tschesche, Harald

Springer

The protein journal 19 (2000), S. 685-692

add to mindlist on the mindlist

Details

ISSN: 1573-4943

Keywords: Fibronectin ; type IV collagenase ; metalloprotease ; TIMP-2

Source: Springer Online Journal Archives 1860-2000

Topics: Chemistry and Pharmacology

Notes: Abstract Human plasma fibronectin (pFN) contains a cryptic metalloprotease present in the collagen-binding domain. The enzyme could be generated and activated in the presence of Ca2+ from the purified 70-kDa pFN fragment produced by cathepsin D digestion. In this work we cloned and expressed the metalloprotease, designated FN type IV collagenase (FnColA), and a truncated variant (FnColB) in E. coli. The recombinant pFN protein fragment was isolated from inclusion bodies, and subjected to folding and autocatalytic degradation in the presence of Ca2+, and yielded an active enzyme capable of digesting gelatin, helical type II and type IV collagen, α- and β-casein, insulin b-chain, and a synthetic Mca-peptide. In contrast, isolated plasma fibronectin, type I collagen, and the DNP-peptide were no substrates. Both catalytically active recombinant pFN fragments were efficiently inhibited by EDTA, and batimastat, and, in contrast to the glycosylated enzyme isolated from plasma fibronectin, were also inhibited by TIMP-2.