Leptomeningeal Carcinomatosis: A Case Report and Literature Review.

Leptomeningeal carcinomatosis (LC) is a rare complication of malignant tumors that involves metastasis to the meninges surrounding the brain and/or spinal cord. The incidence of LC appears to be increasing, which has been attributed to increased survival times of cancer patients and increased diagnostic sensitivity. In this case, we discuss a patient with a history of colon cancer and lung cancer who was admitted with multiple cranial nerve palsies and sensory deficits.

Glu residues of βDELSEED-motif are essential for peptide binding in Escherichia coli ATP synthase.

The current study establishes the necessity of Glu-381, Glu-384, and Glu-385 in the βDELSEED-motif of Escherichia coli ATP synthase for peptide binding and inhibition. Inhibitory profiles of wild type and mutant E. coli membrane bound FF ATP synthase were studied in the presence and absence of C-terminal NH bound melittin.

A Therapeutic Connection between Dietary Phytochemicals and ATP Synthase.

For centuries, phytochemicals have been used to prevent and cure multiple health ailments. Phytochemicals have been reported to have antioxidant, antidiabetic, antitussive, antiparasitic, anticancer, and antimicrobial properties. Generally, the therapeutic use of phytochemicals is based on tradition or word of mouth with few evidence-based studies.

Venom peptides cathelicidin and lycotoxin cause strong inhibition of Escherichia coli ATP synthase.

Venom peptides are known to have strong antimicrobial activity and anticancer properties. King cobra cathelicidin or OH-CATH (KF-34), banded krait cathelicidin (BF-30), wolf spider lycotoxin I (IL-25), and wolf spider lycotoxin II (KE-27) venom peptides were found to strongly inhibit Escherichia coli membrane bound F1Fo ATP synthase. The potent inhibition of wild-type E.

ATP synthase: a molecular therapeutic drug target for antimicrobial and antitumor peptides.

In this review we discuss the role of ATP synthase as a molecular drug target for natural and synthetic antimicrobial/ antitumor peptides. We start with an introduction of the universal nature of the ATP synthase enzyme and its role as a biological nanomotor. Significant structural features required for catalytic activity and motor functions of ATP synthase are described.