Carbonic anhydrase and acetylcholinesterase inhibitory effects of carbamates and sulfamoylcarbamates

Figures & data

Table 1. Human carbonic anhydrase isoenzymes (hCA I and II) inhibition value with carbamate derivatives by an esterase assay with NPA.

	IC50 (nM)		KI (nM)
Compounds	hCA I	hCA II	hCA I	hCA II
1*	319.6	251.9	387.3	196.2
2†	388.0	524.2	264.2	835.7
3*	236.0	259.6	295.7	167.5
4*	244.0	134.2	245.6	378.5
5*	686.0	184.8	893.5	342.8
6†	324.0	251.5	586.5	103.9
7*	300.2	191.0	194.4	176.8
8*	226.2	194.6	207.5	482.0
AZA‡			36.20	3.70

*Sulfamoylcarbamates.

†Carbamate derivatives.

‡AZA was used as positive standard inhibitor for both CA isoenzymes (CA I and II).

Ki values belonging to AZA was expressed as micromolar levels.

Figure 1. The chemical structures of synthesized carbamate derivatives.

Table 2. IC₅₀ values of acetylcholinesterase enzyme (AChE) inhibition parameters of carbamate derivatives comparison with standards rivastigmine (RIV) and galanthamine (GLT).

Compounds	IC50 (nM)	r^2	KI (nM)
1	50.20	0.9754	27.6 ± 12.9
2	29.90	0.9914	12.0 ± 2.0
3	105.40	0.9877	15.5 ± 1.8
4	66.91	0.9776	31.4 ± 7.3
5	69.92	0.9855	61.3 ± 25.9
6	95.78	0.9622	14.4 ± 3.3
7	104.10	0.9819	38.4 ± 5.1
8	94.86	0.9565	57.6 ± 6.9
RIV*	501.00	–	–
GLT*	4.00	–	–

*Rivastigmine (RIV) and galanthamine (GLT) were used as positive standards and obtained from the reference of 37 and expressed as micromolar (μM).