RESUMEN
Amyloid Light chain (AL) amyloidosis is a rare disease, which is seen in approximately one-tenth of patients with multiple myeloma. We report a 52 years old male, who presented with complaints of anorexia and weight loss. He was diagnosed to have multiple myeloma-international staging score (ISS) Stage 3 and was started on VTD (Bortezomib, Thalidomide, and Dexamethasone) chemotherapy. Within 2 weeks of therapy, he had abdominal symptoms like abdominal pain, loose stools, vomiting and hematochezia. Imaging showed dilated proximal bowel loops with fluid filled contents and prominent vessels in rectum. Emergency surgical exploration revealed thickened proximal jejunum with blood clots in the lumen. Resection of proximal jejunum was done. Histopathological examination of resected specimen was suggestive of AL amyloidosis. Post-surgical resection of jejunum, patient had initial improvement followed by deterioration. He was discharged against medical advice as per relative’s request. Hence an index of clinical suspicion of amyloidosis must been present in all Multiple myeloma patients.
RESUMEN
It is well known that water molecules play an indispensable role in the structure and function of biological macromolecules. The water-mediated ionic interactions between the charged residues provide stability and plasticity and in turn address the function of the protein structures. Thus, this study specifically addresses the number of possible water-mediated ionic interactions, their occurrence, distribution and nature found in 90% non-redundant protein chains. Further, it provides a statistical report of different charged residue pairs that are mediated by surface or buried water molecules to form the interactions. Also, it discusses its contributions in stabilizing various secondary structural elements of the protein. Thus, the present study shows the ubiquitous nature of the interactions that imparts plasticity and flexibility to a protein molecule.