The Interfacial Interactions of Glycine and Short Glycine Peptides in Model Membrane Systems |
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| Authors: | Kaitlin A Doucette Prangthong Chaiyasit Donn L Calkins Kayli N Martinez Cameron Van Cleave Callan A Knebel Anan Tongraar Debbie C Crans |
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| Affiliation: | 1.Cell and Molecular Biology Program, Colorado State University, Fort Collins, CO 80523, USA;2.Department of Chemistry, Colorado State University, Fort Collins, CO 80523, USA; (D.L.C.); (K.N.M.); (C.V.C.); (C.A.K.);3.School of Chemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand; (P.C.); (A.T.) |
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| Abstract: | 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. |
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| Keywords: | glycine reverse micelles AMPs pKa 1H NMR |
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