Aminoisobutyric acid (Aib) and its homologues are strong helix promoters in peptide mimetics. Particularly in combination with cationic amino acids (arginine and lysine), amphiphilic Aib-containing model peptides show high cellular uptake combined with potent resistance to trypsin, pronase and other proteases. Crossing cell membranes, diffusion into the cytoplasm and slightly even into the nucleus without exerting any cytotoxicity have been published for a number of Aib peptide mimetics in recent years for applications in cancer treatment, antimicrobial peptides and cell penetrating peptides (CPP).

We offer Aib and its homologues positioning the dimethyl fragment either close to the N- or to the C-terminus.

• Aib-based peptide backbone as scaffolds for helical peptide mimics; R. Banerjee, G. Basu, P. Chène, S. Roy; J. Peptide Res. 2002; 60: 88–94.
• Cellular uptake of Aib-containing amphipathic helix peptide; S. Wada, H. Tsuda, T. Okada, H. Urata; Bioorganic & Medicinal Chemistry Letters 2011; 21(19): 5688–5691.
• Design and synthesis of cationic Aib-containing antimicrobial peptides: conformational and biological studies; S. Zikou, A. Koukkou, P. Mastora, M. Sakarellos-Daitsiotis, C. Sakarellos, C. Drainas, E. Panou-Pomonis; J.Pept.Sci. 2007; 13(7): 481-6.