Thymosinα1 is a peptidic hormone with pleiotropic activity, which is used in the therapy of several diseases. It is unstructured in water solution and interacts with negative regions of micelles and vesicles assuming two tracts of helical conformation with a structural flexible break in between. The studies of the interaction of Thymosinα1 with micelles of mixed dipalmitoylphosphatidylcholine and sodium dodecylsulfate and vesicles with mixed dipalmitoylphosphatidylcholine/dipalmitoylphosphatidylserine, the latter the negative component of the membranes, by (1)H and natural abundance (15)N NMR are herewith reported, reviewed, and discussed. The results indicate that the preferred interactions are those where the surface is negatively charged due to sodium dodecylsulfate or due to the presence of dipalmitoylphosphatidylserine exposed on the surface. In fact the unbalance of dipalmitoylphosphatidylserine on the cellular surface is an important phenomenon present in pathological conditions of cells. Moreover, the direct interaction of Thymosinα1 with K562 cells presenting an overexposure of phosphatidylserine as a consequence of resveratrol-induced apoptosis was carried out.

Nepravishta, R., Pica, F., Garaci, E., Paci, M., Mandaliti, W., SINIBALDI VALLEBONA, P. (2016). Mechanism of action of thymosinα1: does it interact with membrane by recognition of exposed phosphatidylserine on cell surface? A structural approach. In Thymosins (pp. 101-119). Gerald Litwack [10.1016/bs.vh.2016.04.002].

Mechanism of action of thymosinα1: does it interact with membrane by recognition of exposed phosphatidylserine on cell surface? A structural approach

PICA, FRANCESCA;GARACI, ENRICO;PACI, MAURIZIO;SINIBALDI VALLEBONA, PAOLA
2016-01-01

Abstract

Thymosinα1 is a peptidic hormone with pleiotropic activity, which is used in the therapy of several diseases. It is unstructured in water solution and interacts with negative regions of micelles and vesicles assuming two tracts of helical conformation with a structural flexible break in between. The studies of the interaction of Thymosinα1 with micelles of mixed dipalmitoylphosphatidylcholine and sodium dodecylsulfate and vesicles with mixed dipalmitoylphosphatidylcholine/dipalmitoylphosphatidylserine, the latter the negative component of the membranes, by (1)H and natural abundance (15)N NMR are herewith reported, reviewed, and discussed. The results indicate that the preferred interactions are those where the surface is negatively charged due to sodium dodecylsulfate or due to the presence of dipalmitoylphosphatidylserine exposed on the surface. In fact the unbalance of dipalmitoylphosphatidylserine on the cellular surface is an important phenomenon present in pathological conditions of cells. Moreover, the direct interaction of Thymosinα1 with K562 cells presenting an overexposure of phosphatidylserine as a consequence of resveratrol-induced apoptosis was carried out.
2016
Settore MED/07 - MICROBIOLOGIA E MICROBIOLOGIA CLINICA
Settore BIO/10 - BIOCHIMICA
English
Rilevanza internazionale
Capitolo o saggio
hormones; NMR spectroscopy; peptide membrane interaction; thymic hormones; thymosinα1
Nepravishta, R., Pica, F., Garaci, E., Paci, M., Mandaliti, W., SINIBALDI VALLEBONA, P. (2016). Mechanism of action of thymosinα1: does it interact with membrane by recognition of exposed phosphatidylserine on cell surface? A structural approach. In Thymosins (pp. 101-119). Gerald Litwack [10.1016/bs.vh.2016.04.002].
Nepravishta, R; Pica, F; Garaci, E; Paci, M; Mandaliti, W; SINIBALDI VALLEBONA, P
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/174290
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