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...
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doaj-5d10122762a94d23b8fdde6da687979d2020-12-27T00:00:29ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-12-012216216210.3390/ijms22010162The Interfacial Interactions of Glycine and Short Glycine Peptides in Model Membrane SystemsKaitlin A. Doucette0Prangthong Chaiyasit1Donn L. Calkins2Kayli N. Martinez3Cameron Van Cleave4Callan A. Knebel5Anan Tongraar6Debbie C. Crans7Cell and Molecular Biology Program, Colorado State University, Fort Collins, CO 80523, USASchool of Chemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima 30000, ThailandDepartment of Chemistry, Colorado State University, Fort Collins, CO 80523, USADepartment of Chemistry, Colorado State University, Fort Collins, CO 80523, USADepartment of Chemistry, Colorado State University, Fort Collins, CO 80523, USADepartment of Chemistry, Colorado State University, Fort Collins, CO 80523, USASchool of Chemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima 30000, ThailandCell and Molecular Biology Program, Colorado State University, Fort Collins, CO 80523, USAThe 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 <sup>1</sup>H 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.https://www.mdpi.com/1422-0067/22/1/162glycinereverse micellesAMPspK<sub>a</sub><sup>1</sup>H NMR |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Kaitlin A. Doucette Prangthong Chaiyasit Donn L. Calkins Kayli N. Martinez Cameron Van Cleave Callan A. Knebel Anan Tongraar Debbie C. Crans |
spellingShingle |
Kaitlin A. Doucette Prangthong Chaiyasit Donn L. Calkins Kayli N. Martinez Cameron Van Cleave Callan A. Knebel Anan Tongraar Debbie C. Crans The Interfacial Interactions of Glycine and Short Glycine Peptides in Model Membrane Systems International Journal of Molecular Sciences glycine reverse micelles AMPs pK<sub>a</sub> <sup>1</sup>H NMR |
author_facet |
Kaitlin A. Doucette Prangthong Chaiyasit Donn L. Calkins Kayli N. Martinez Cameron Van Cleave Callan A. Knebel Anan Tongraar Debbie C. Crans |
author_sort |
Kaitlin A. Doucette |
title |
The Interfacial Interactions of Glycine and Short Glycine Peptides in Model Membrane Systems |
title_short |
The Interfacial Interactions of Glycine and Short Glycine Peptides in Model Membrane Systems |
title_full |
The Interfacial Interactions of Glycine and Short Glycine Peptides in Model Membrane Systems |
title_fullStr |
The Interfacial Interactions of Glycine and Short Glycine Peptides in Model Membrane Systems |
title_full_unstemmed |
The Interfacial Interactions of Glycine and Short Glycine Peptides in Model Membrane Systems |
title_sort |
interfacial interactions of glycine and short glycine peptides in model membrane systems |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1661-6596 1422-0067 |
publishDate |
2021-12-01 |
description |
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 <sup>1</sup>H 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. |
topic |
glycine reverse micelles AMPs pK<sub>a</sub> <sup>1</sup>H NMR |
url |
https://www.mdpi.com/1422-0067/22/1/162 |
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