The Interfacial Interactions of Glycine and Short Glycine Peptides in Model Membrane Systems.
The interactions of amino acids and peptides at model membrane interfaces have considerable implications for biological functions, with the ability to act as chemical messengers, hormones, neurotransmitters, and even as antibiotics and anticancer agents. In this study, glycine and the short glycine peptides diglycine, triglycine, and tetraglycine are studied with regards to their interactions at the model membrane interface of Aerosol-OT (AOT) reverse micelles via 1H NMR spectroscopy, dynamic light scattering (DLS), and Langmuir trough measurements. It was found that with the exception of monomeric glycine, the peptides prefer to associate between the interface and bulk water pool of the reverse micelle. Monomeric glycine, however, resides with the N-terminus in the ordered interstitial water (stern layer) and the C-terminus located in the bulk water pool of the reverse micelle.
['Doucette|Kaitlin A|KA|', 'Chaiyasit|Prangthong|P|', 'Calkins|Donn L|DL|', 'Martinez|Kayli N|KN|', 'Van Cleave|Cameron|C|0000-0002-0924-1738', 'Knebel|Callan A|CA|', 'Tongraar|Anan|A|', 'Crans|Debbie C|DC|0000-0001-7792-3450']
D005998:Glycine D006033:Glycylglycine D008566:Membranes D008823:Micelles D008962:Models, Theoretical D009842:Oligopeptides D010446:Peptide Fragments D014867:Water
glycine reverse micelles 1H NMR AMPs pKa