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Hyaluronan-Arginine Interactions—An Ultrasound and ITC Study

High-resolution ultrasound spectroscopy and isothermal titration calorimetry were used to characterize interactions between hyaluronan and arginine oligomers. The molecular weight of arginine oligomer plays an important role in interactions with hyaluronan. Interactions were observable for arginine...

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Detalles Bibliográficos
Autores principales: Jugl, Adam, Pekař, Miloslav
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7570013/
https://www.ncbi.nlm.nih.gov/pubmed/32932626
http://dx.doi.org/10.3390/polym12092069
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author Jugl, Adam
Pekař, Miloslav
author_facet Jugl, Adam
Pekař, Miloslav
author_sort Jugl, Adam
collection PubMed
description High-resolution ultrasound spectroscopy and isothermal titration calorimetry were used to characterize interactions between hyaluronan and arginine oligomers. The molecular weight of arginine oligomer plays an important role in interactions with hyaluronan. Interactions were observable for arginine oligomers with eight monomer units and longer chains. The effect of the ionic strength and molecular weight of hyaluronan on interactions was tested. In an environment with increased ionic strength, the length of the arginine oligomer was crucial. Generally, sufficiently high ionic strength suppresses interactions between hyaluronan and arginine oligomers, which demonstrated interactions in water. From the point of view of the molecular weight of hyaluronan, the transition between the rod conformation and the random coil conformation appeared to be important.
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spelling pubmed-75700132020-10-29 Hyaluronan-Arginine Interactions—An Ultrasound and ITC Study Jugl, Adam Pekař, Miloslav Polymers (Basel) Article High-resolution ultrasound spectroscopy and isothermal titration calorimetry were used to characterize interactions between hyaluronan and arginine oligomers. The molecular weight of arginine oligomer plays an important role in interactions with hyaluronan. Interactions were observable for arginine oligomers with eight monomer units and longer chains. The effect of the ionic strength and molecular weight of hyaluronan on interactions was tested. In an environment with increased ionic strength, the length of the arginine oligomer was crucial. Generally, sufficiently high ionic strength suppresses interactions between hyaluronan and arginine oligomers, which demonstrated interactions in water. From the point of view of the molecular weight of hyaluronan, the transition between the rod conformation and the random coil conformation appeared to be important. MDPI 2020-09-12 /pmc/articles/PMC7570013/ /pubmed/32932626 http://dx.doi.org/10.3390/polym12092069 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Jugl, Adam
Pekař, Miloslav
Hyaluronan-Arginine Interactions—An Ultrasound and ITC Study
title Hyaluronan-Arginine Interactions—An Ultrasound and ITC Study
title_full Hyaluronan-Arginine Interactions—An Ultrasound and ITC Study
title_fullStr Hyaluronan-Arginine Interactions—An Ultrasound and ITC Study
title_full_unstemmed Hyaluronan-Arginine Interactions—An Ultrasound and ITC Study
title_short Hyaluronan-Arginine Interactions—An Ultrasound and ITC Study
title_sort hyaluronan-arginine interactions—an ultrasound and itc study
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7570013/
https://www.ncbi.nlm.nih.gov/pubmed/32932626
http://dx.doi.org/10.3390/polym12092069
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