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A new coumarin based Schiff-base chemosensor-(E)-7-(((8-Hydroxyquinoline-2-yl) methylene) amino)-4-(trifluoromethyl)-2H-chromen-2-one (H 12 L) was designed and synthesized. This chemosensor was evaluated as a colorimetric sensor for Fe 3+ and fluorescence "turn on-off" response of Zn 2+ and Cu 2+ using steady-state absorption and fluorescence spectroscopy. In presence of Fe 3+ and Zn 2+ , the absorption intensity as well as the fluorescence emission intensity increases drastically compared to other survey metal ions, with a distinct color change which provide naked eye detection. However, in presence of Cu 2+ , it also exhibits quenching of fluorescence emission intensity which may be due to paramagnetic nature of Cu 2+ ion. The stoichiometric ratio and binding constant were calculated using Benesi-Hildebrand relation and Job's plot analyses giving 1:1 stoichiometry. The interaction and binding nature of H 12 L with Zn 2+ ion was further confirmed by 1 H NMR titration assay and ESI-Mass spectral analysis. The reversibility nature of H 12 L was also studied using EDTA as a chelating ligand. Moreover, H 12 L exhibits two INHIBIT logic gates with two different chemical inputs (i) Zn 2+ (IN1) and Cu 2+ (IN2) and (ii) Zn 2+ (IN1) and EDTA (IN2) and the emission as output. Again, an IMPLICATION logic gate is obtained with Cu 2+ and EDTA as chemical inputs and emission as output mode. Both H 12 L and metal-complexes were optimized using density functional theory and vibrational frequency calculations confirm that both are at local minima on the potential energy surfaces. The corresponding energy difference between HOMO and LUMO of H 12 L, Zn-complex and Cu-complex are found to be 2.11, 0.81 and 0.17 eV, respectively.A new coumarin based Schiff-base chemosensor has been synthesized and characterized Evaluated as a colorimetric sensor for Fe 3+ and fluorescence turn on-off response of Zn 2+ and Cu 2+ Both Benesi-Hildebrand relation and Job's plot analyses gives 1:1 stoichiometry Free ligand can be reusable and recyclable by treating the complex probe with EDTA Binary logic function of two INHIBIT with an IMPLICATION logic gate is anticipated

Background: Joint mobilization is an effective intervention for adhesive capsulitis. Scapular Mobilization in shoulder adhesive capsulitis is used to decrease intra articular pressure by increasing mobility of the joint capsule and its surrounding soft tissue that results in a reduction of pain and increase range of motion and shoulder function. At the same time the use of mobilization with movement (MWM) for peripheral joints was also used clinically. This technique combines a sustained application of a manual technique 'gliding' force to a joint with concurrent physiologic motion of joint, either actively performed by the subject or passively performed by the therapist. So far there is no study which is done on comparison between both of these techniques. The aim of the study is to find out whether the scapular mobilization or mobilization with movement technique improve gleno-humeral range of motion and reduce pain in patients with shoulder adhesive capsulitis.Methods: 50 subjects with adhesive capsulitis were randomly divided in to two groups and one group was treated with mobilization with movement and another group treated with scapular mobilization technique. Each group consist 25 patients. Both groups were given hot packs and pendular exercises as conventional therapy procedures. Treatment was given 5 days a week for 3 weeks. Restricted joint range of motion and severity of pain were measured before and after treatment completion by using goniometer and SPADI pain score respectively.Result: Results of the present study revealed that there was a significant difference in SPADI pain score(%), AROM-GH-Flexion and AROM-GH-External rotation who were treated in group A(MWM) with mean being 44.00, 102.24 and 46.08 respectively compared to group B (SM) with mean being 54.00, 81.00 and 35.84 in 3 weeks. Comparisons between these three parameters used in two treatment techniques were extremely significant (p= 0.000 for all). Conclusion:On the basis of the results, it can be concluded that, the present study provided evidence to support the use of physical therapy regimen for shoulder adhesive capsulitis in the form of mobilization with movement and scapular mobilization in reduction of pain and improvement of glenohumeral range of motion in terms of SPADI pain scale(%) and AROM respectively. In addition results support that mobilization with movement showed better result as compared to scapular mobilization in 3 weeks.

Interaction of monooaqua and diaqua ruthenium complexes such as, [trans-RuCl 3 (H 2 O)(3H-imidazole)(dmso-S)] I, [trans-RuCl 2 (H 2 O) 2 (3H-imidazole)(dmso-S)] +1 II, [trans-RuCl 3 (H 2 O)(4-amino-1,2,4-triazole)(dmso-S)] III and trans-RuCl 2 (H 2 O) 2 (4-amino-1,2,4-triazole)(dmso-S)] +1 IV, which are formed after intracellular aquation of their respective complexes, with human serum albumin (HSA) has been computationally investigated by molecular docking and two layer QM/MM hybrid methods. The computed binding energy of monoaqua adduct I-HSA and III-HSA evaluated by docking simulation are found to be -4.52 kcalmol -1 and -4.58 kcalmol -1 whereas the binding energy of diaqua adducts II-HSA and IV-HSA are evaluated to be -4.74 kcalmol -1 and -4.91 kcalmol -1 , respectively. Docking results also show that the ruthenium atoms of all the complexes are actively involved in coordination with histidyl nitrogen atoms in the active site of protein. In addition, in order to probe the stabilities of monoaqua and diaqua ruthenium complexes in the active site of protein, we have calculated their energetic by two layer QM/MM method. QM/MM study suggests higher stability of diaqua adduct, II-HSA. The stability of adducts varies in the order: II-HSA> IV-HSA> I-HSA> III-HSA. Binding energy values of all the complexes increase with the incorporation of solvent effect. Thus molecular docking and QM/MM resultsshow that ruthenium complexes interact with the protein receptor more rapidly after their second hydrolysis. Hence, docking as well as ONIOM results will be highly beneficial for providing insight into the molecular mechanism of ruthenium complexes with protein receptor.