pyrularia edulis/tryptophan

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Pyrularia thionin binding to and the role of tryptophan-8 in the enhancement of phosphatidylserine domains in erythrocyte membranes.

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Ingia / Ingia

Pyrularia thionin is a small, strongly basic peptide which interacts readily with cellular and synthetic membranes. With cells it induces hemolysis, depolarizes the cellular membrane with an accompanying influx of Ca2+, and activates an endogenous phospholipase A2. Evidence points toward a binding

Interactions of thionin from Pyrularia pubera with dipalmitoylphosphatidylglycerol large unilamellar vesicles.

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Ingia / Ingia

The peptide toxin thionin from Pyrularia pubera binds to dipalmitoylphosphatidylglycerol (DPPG) large unilamellar vesicles as shown by an increase in the intensity and blue-shift of the fluorescence emission spectrum of the single tryptophan residue of the protein. The magnitude of these

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Herbal & Natural Medicine

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