The Interfacial Interactions of Glycine and Short Glycine Peptides in Model Membrane Systems

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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Main Authors: Kaitlin A. Doucette, Prangthong Chaiyasit, Donn L. Calkins, Kayli N. Martinez, Cameron Van Cleave, Callan A. Knebel, Anan Tongraar, Debbie C. Crans
Format: Article
Language:English
Published: MDPI AG 2021-12-01
Series:International Journal of Molecular Sciences
Subjects:
glycine
reverse micelles
AMPs
pK<sub>a</sub>
<sup>1</sup>H NMR
Online Access:https://www.mdpi.com/1422-0067/22/1/162
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spelling 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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