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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Bibliographic Details
Published in:International journal of molecular sciences 2020-12, Vol.22 (1), p.162
Main Authors: Doucette, Kaitlin A, Chaiyasit, Prangthong, Calkins, Donn L, Martinez, Kayli N, Van Cleave, Cameron, Knebel, Callan A, Tongraar, Anan, Crans, Debbie C
Format: Article
Language:English
Subjects:
1H NMR
AMPs
Antibiotics
C-Terminus
Cancer
Glycine
Hormones
Interfaces
Investigations
Light scattering
Lipids
Magnetic resonance spectroscopy
Membranes
Micelles
N-Terminus
Neurotransmitters
NMR
NMR spectroscopy
Nuclear magnetic resonance
Peptides
Photon correlation spectroscopy
pKa
Reverse micelles
Spectrum analysis
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Summary: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 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.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms22010162