New studies about the insertion mechanism of Thymosin α1 in negative regions of model membranes as starting point of the bioactivity

Amino Acids
Walter MandalitiM Paci

Abstract

Thymosin α1 is a peptidic hormone already used in the therapy of several diseases. Until now, the description of the precise receptor and mechanism for its action still remains elusive. The interaction of Thymosin α1, which is unstructured in water solution, has been recently studied in sodium dodecylsulphate micellar systems and it was reported that Thymosin α1 inserts in micelle assuming a conformation with two tracts of helix with a structural break in between. An investigation of its interaction both with micelles of dodecylphosphocholine alone and with mixed dodecylphosphocholine-sodium dodecylsulphate micelles is here reported. In these environments the results indicate that Thymosin α1 in phospholipidic membrane exposing choline polar heads interacts by aspecific modality and, oppositely, in the mixed dodecylphosphocholine-sodium dodecylsulphate micelles an insertion in the micellar hydrophobic region conformationally similar to that found in sodium dodecylsulphate micelles occurs. In presence of mixed micelles the insertion and structuration occur in preferred regions when the membrane models are negatively charged. From the point of view of the mechanism of action, insertion its N terminus in negative regions of membra...Continue Reading

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Citations

Oct 28, 2017·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Walter MandalitiMaurizio Paci
Jan 21, 2017·Future Microbiology·Claudia MatteucciEnrico Garaci
Aug 1, 2018·Expert Opinion on Biological Therapy·Walter MandalitiMaurizio Paci
Jun 27, 2018·Nature Medicine·Luigina RomaniEnrico Garaci

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