1.D.81.  The Synthetic Tetrapeptide Amphiphile (TPA) Family 

Basak et al. 2017 reported a minimalistic tetrapeptide amphiphile (MPA1), derived from alanine and aminopicolinic acid that forms cation selective pores in lipid bilayers. A dimeric structure appears to form the ion-transporting pore. The pore shows a preference for Na+ owing to the oligoether chain at the C-terminus. These tetrapeptide scaffolds have a long open lifetime. Such small peptides containing pyridine can potentially be utilized for pH modulated ion transport. The basic scaffold is shown below.

Pore forming tetrapeptide scaffold.

Pore forming tetrapeptide scaffold.



 

References:

Basak, D., S. Sridhar, A.K. Bera, and N. Madhavan. (2017). A minimalistic tetrapeptide amphiphile scaffold for transmembrane pores with a preference for sodium. Bioorg Med Chem Lett. [Epub: Ahead of Print]