Dynamical system analysis of FLRW models with Modified Chaplygin gas.

We investigate Friedmann-Lamaitre-Robertson-Walker (FLRW) models with modified Chaplygin gas and cosmological constant, using dynamical system methods. We assume [Formula: see text] as equation of state where [Formula: see text] is the matter-energy density, p is the pressure, [Formula: see text] is a parameter which can take on values [Formula: see text] as well as A and [Formula: see text] are positive constants. We draw the state spaces and analyze the nature of the singularity at the beginning, as well as the fate of the universe in the far future. In particular, we address the question whether there is a solution which is stable for all the cases.

Synthesis of novel tris-chalcones and determination of their inhibition profiles against some metabolic enzymes.

In this study, we report the synthesis of novel tris-chalcones and testing of human carbonic anhydrase I, and II isoenzymes (hCA I, and hCA II), acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and α-glycosidase (α-Gly) inhibitors for the development of novel chalcone structures towards for treatment of some diseases. The compounds demonstrated Ki values between 13.6 ± 1.1 and 50.0 ± 17.1 nM on hCA I, 9.9 ± 0.8 and 39.5 ± 15.1 nM on hCA II, 3.1 ± 0.2 and 20.1 ± 1.9 nM on AChE, 4.9 ± 0.4 and 14.7 ± 5.2 nM on BChE and 3.9 ± 0.2 and 22.4 ± 10.7 nM on α-Gly enzymes. The results revealed that novel tris-chalcones can have promising drug potential for glaucoma, leukaemia, epilepsy; Alzheimer's disease that was associated with the high enzymatic activity of hCA I, hCA II, AChE, and BChE enzymes.

Synthesis and biological evaluation of novel tris-chalcones as potent carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase and α-glycosidase inhibitors.

A novel class of fluoro-substituted tris-chalcones derivatives (5a-5i) was synthesized from phloroglucinol and corresponding benzaldehydes. A three step synthesis method was followed for the production of these tris-chalcone compounds. The structures of the newly synthesized compounds (5a-5i) were confirmed on the basis of IR, 1H NMR, 13C NMR, and elemental analysis.The compounds' inhibitory activities were tested against human carbonic anhydrase I and II isoenzymes (hCA I and hCA II), acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and α-glycosidase (α-Gly). These chalcone derivatives had Ki values in the range of 19.58-78.73 nM for hCA I, 12.23-41.70 nM for hCA II, 1.09-6.84 nM for AChE, 8.30-32.30 nM for BChE and 0.93 ±â€¯0.20-18.53 ±â€¯5.06 nM against α-glycosidase. These results strongly support the promising nature of the tris-chalcone scaffold as selective carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase, and α-glycosidase inhibitor. Overall, due to these derivatives' inhibitory potential on the tested enzymes, they are promising drug candidates for the treatment of diseases like glaucoma, leukemia, epilepsy; Alzheimer's disease; type-2 diabetes mellitus that are associated with high enzymatic activity of carbonic anhydrase, acetylcholine esterase, butyrylcholinesterase, and α-glycosidase.

Synthesis of two phloroglucinol derivatives with cinnamyl moieties as inhibitors of the carbonic anhydrase isozymes I and II: an in vitro study.

Two cinnamyl-substituted phloroglucinols, 4-p-methoxycinnamyl phloroglucinol (9) and 4,6-bis-p-methoxycinnamyl phloroglucinol (10) were synthesized. Two carbonic anhydrases, human carbonic anhydrase I and II (hCA I and II), were purified. Kinetic interactions between these isozymes with 9 and 10 were investigated. These new compounds exhibited inhibitory effects on the hCA I and II enzymes' activity in vitro. The combination of the inhibitory effects of both phloroglucinol and p-coumaric acid groups in a single compound was explored. However, relative to the inhibitory effects of the two groups separately, compounds 9 and 10 demonstrated comparable inhibitory effects. More effective inhibitors of CAs could be created by testing these compounds on other CA isozymes.