In this work, we investigate the structure, dynamic and thermodynamic properties of noncanonical disubstituted amino acids (alpha,alpha-dialkyl glycines), also known as non-natural amino acids, in the peptaibol Alamethicin. The amino acids under study are Aib (alpha-amino isobutyric acid or alpha-methyl alanine), Deg (alpha,alpha-diethyl glycine), Dpg (alpha,alpha-dipropyl glycine), Dibg (alpha,alpha-di-isobutyl glycine), Dhg (alpha,alpha-dihexyl glycine), D Phi g (alpha,alpha-diphenyl glycine), Db(z)g (alpha,alpha-dibenzyl glycine), Ac(6)c (alpha,alpha-cyclohexyl glycine), and Dmg (alpha,alpha-dihydroxymethyl glycine). It is hypothesized that these amino acids are able to induce well-defined secondary structure in peptidomimetics. To test this hypothesis, new peptidomimetics of Alamethicin were constructed by replacing the native Aib positions of Alamethicin by one or more new alpha,alpha-dialkyl glydnes. Dhg and Ac(6)c demonstrated the capacity to induce well-defined alpha-helical structures. Dhg and Ac(6)c also promote the thermodynamic stabilization of these peptides in a POPC model membrane and are better alternatives to the Aib in Alamethicin. These noncanonical amino acids also improved secondary structure properties, revealing preorganization in water and maintenance of alpha helical structure in POPC. We show that it is possible to optimize the helicity and thermodynamic properties of native Alamethicin, and we suggest that these amino acids could be incorporated in other peptides with similar structural effect.