Amyloid aggregation and secondary structure changes of liver cystatin: Acidic denaturation and TFE induced studies.

A cysteine proteinase inhibitor has been purified by affinity chromatography from the liver of buffalo. Liver cystatin is subjected to incubation at low pH with co-solvent TFE, where we have studied the effect on the conformation, activity and tendency to form aggregates or fibrils. ANS fluorescence was used to study conformational changes.

In vitro reconstitution of interactions in the CARD9 signalosome.

The caspase-associated recruitment domain (CARD)‑containing protein 9 (CARD9) signalosome is composed of CARD9, B‑cell CLL/lymphoma 10 (BCL10) and mucosa‑associated lymphoid tissue lymphoma translocation protein 1 (MALT1). The CARD9 signalosome has been reported to exert critical functions in the immunoreceptor tyrosine‑based activation motif‑coupled receptor‑mediated activation of myeloid cells, through nuclear factor‑κB pathways during innate immunity processes. During CARD9 signalosome assembly, BCL10 has been revealed to function as an adaptor protein and to interact with CARD9 via CARD‑CARD interactions; BCL10 also interacts with MALT1 via its C‑terminal Ser/Thr‑rich region and the first immunoglobulin domain of MALT1.

Glycation of Liver Cystatin: Implication on its Structure and Function.

The increased level of reducing sugars and their derivatives in a diabetic condition has been the main cause of protein related complications. The changes in native state of proteins upon glycation induce loss in the function and structure of proteins. This further leads to cell damage and accumulation of immune system inducing AGE formation.

Bilirubin binding with liver cystatin induced structural and functional changes.

Cysteine proteinases and their inhibitors play a significant role in the proteolytic environment of the cells. Inhibitors of cysteine proteinases regulate the activity of these enzymes helping in checking the degdration activity of cathepsins. The bilirubin secreated by liver cells can bind to cystatin present in the liver resulting in its functional inactivation, which may further lead to the increase in cathepsins level causing liver cirrhosis.

Synthesis, molecular docking and biological evaluation of new steroidal 4H-pyrans.

A series of new steroidal 4H-pyrans (4-6) have been synthesized from steroidal α, β-unsaturated ketones (1-3). The products (4-6) were characterized by IR, (1)H NMR, (13)C NMR, MS and analytical data. The interaction studies of compounds (4-6) with DNA were carried out by employing gel electrophoresis, UV-vis and fluorescence spectroscopy.