The title compound, C(10)H(7)Cl(3)O, obtained as a major byproduct from a classical Schmidt reaction. The cyclohexyl ring is distorted from a classical chair conformation, as observed for monocyclic analogues, presumably due to conjugation of the planar annulated benzo ring and the ketone group (r.m.s. deviation 0.024 Å). There are no significant intermolecular interactions.

The host-guest interaction of a series of cyclohexyl-appended guests with cucurbit[8]uril (Q[8]) was studied by ¹H NMR spectroscopy, isothermal titration calorimetry (ITC), and X-ray crystallography. The X-ray structure revealed that two cycloalkane moieties can be simultaneously encapsulated in the hydrophobic cavity of the Q[8] host to form a ternary complex for the first time.

The mol-ecule of the title compound, C(30)H(46), has a crystallographically imposed inversion center and the cyclo-hexyl groups are oriented with their methine H atoms pointing towards one another (H⋯H = 1.99 Å). The cyclohexyl groups adopt chair conformations. A significant C-H⋯π inter-action assembles mol-ecules into layers parallel to (100).

A simple and Noval Synthesis of guanidine derivatives is presented in this study. The construction of the Central basic Scaffolds is achieved by the using of HgCl2 as a promoter. The Formation of product of substituted guanidines controlled by amount of reactant. Further a new fast-tract access to N-1(Boc)-N-(2) cyclohexyl-N(3) phenyl-guanidine was developed.

In the title compound, C(14)H(17)NO(3), the plane of the phenyl ring and the least-squares plane of the cyclo-hexyl moiety enclose an angle of 89.14 (6)°. The cyclohexyl ring adopts a chair conformation. In the crystal, the molecules are linked by weak C-H⋯O bonds, with each of the nitro-O atoms accepting two such interactions.

Five substituted amides of lysine with the general formula: X-Lys-NH-Y, where X= acetyl or ethoxycarbonyl, Y= cyclohexyl, benzyl, hexyl or cadaverine residue were synthesised and their effects on fibrinolytic activity of plasmin, clotting activity of thrombin and amidolytic activities of both enzymes were examined.