title: Mechanism of Action of Thymosinα1: Does It Interact with Membrane by Recognition of Exposed Phosphatidylserine on Cell Surface? A Structural Approach.
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.
authors.affiliation: University of Rome "Tor Vergata", Rome, Italy; Faculty of Pharmacy Catholic University "Our Lady of Good Counsel", Tirane, Albania.
authors.forename: R
authors.initials: R
authors.lastname: Nepravishta
authors.affiliation: University of Rome "Tor Vergata", Rome, Italy.
authors.forename: W
authors.initials: W
authors.lastname: Mandaliti
authors.affiliation: University of Rome "Tor Vergata", Rome, Italy.
authors.forename: P S
authors.initials: PS
authors.lastname: Vallebona
authors.affiliation: University of Rome "Tor Vergata", Rome, Italy.
authors.forename: F
authors.initials: F
authors.lastname: Pica
authors.affiliation: University of Rome "Tor Vergata", Rome, Italy; San Raffaele Pisana Scientific Institute for Research, Hospitalization and Health Care, Rome, Italy.
authors.forename: E
authors.initials: E
authors.lastname: Garaci
authors.affiliation: University of Rome "Tor Vergata", Rome, Italy. Electronic address: paci@uniroma2.it.
authors.forename: M
authors.initials: M
authors.lastname: Paci
mesh_terms: D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism; D002942:Circular Dichroism; D003903:Deuterium; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008823:Micelles; D008958:Models, Molecular; D015394:Molecular Structure; D010718:Phosphatidylserines / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D012996:Solutions; D000077596:Thymalfasin; D013947:Thymosin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D014270:Trifluoroethanol
chemical_list: D008823:Micelles; D010718:Phosphatidylserines; D012996:Solutions; D013947:Thymosin; D014270:Trifluoroethanol; D003903:Deuterium; D000077596:Thymalfasin
keywords: Hormones; NMR spectroscopy; Peptide membrane interaction; Thymic hormones; Thymosinα1