MOLECULAR DYNAMICS OF THYMOSIN α-1: STRUCTURE STABILIZATION BY PEO-DIAMINE STAPLING

Carlo Schillaci, Alessia Bellomaria, Celeste Santone, Walter Mandaliti, Entela Haloçi, Enver Mustafaj, Ridvan Nepravishta

Abstract


Thymosin α-1 belongs to the small molecule family of thymosines, which have been studied for a long time as molecules with very high potential use as drugs. In particular Thymosin α-1 is under intensive studies for its use in different disorders and diseases such as respiratory distress syndrome, hepatitis C, hepatitis B, AIDS, cyto-megallovirus infection etc. Thymosin α-1 is implicated in the control of gene expression of MHC I, MHC II, cytokines and other immune system regulators, but its molecular mechanism remains still unclear. On the other hand several studies were conducted with the aim to identify the structure of the peptide. In fact it was found that thymosin α-1 presents an α-helix conformation in fluorinated alcool/water mixtures but it is highly unstructured in water solution. It is also presumed that very likely thymosin α-1 presents an α-helix conformation when bound to the receptor. Here we present a MD simulation of a Poly Ethylen Oxide Diamine stapled thymosin α-1 as a new strategy for the stabilization of its α-helix conformation in water solution. The PEO diamine stapled peptide presented a good overall stability also at high temperatures offering new insights into the design of more potent Thymosin α-1 derivative molecules.

Keywords


Thymosin alpha 1; alpha helix; Molecular Dynamics

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Copyright (c) 2014 Ridvan Nepravishta

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