Computational Study of Complex Formation between Hyaluronan Polymers and Polyarginine Peptides at Various Ratios

Hyaluronic acid, a naturally occurring carbohydrate biopolymer in human tissues, finds wide application in cosmetics, medicine, and material science. Its anionic properties play a crucial role in its interaction with positively charged macromolecules and ions. Among these macromolecules, positively...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 39(2023), 40 vom: 10. Okt., Seite 14212-14222
1. Verfasser: Kulik, Natalia (VerfasserIn)
Weitere Verfasser: Minofar, Babak, Jugl, Adam, Pekař, Miloslav
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2023
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't polyarginine 25212-18-4 Hyaluronic Acid 9004-61-9 Polymers Peptides Macromolecular Substances Arginine 94ZLA3W45F
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520 |a Hyaluronic acid, a naturally occurring carbohydrate biopolymer in human tissues, finds wide application in cosmetics, medicine, and material science. Its anionic properties play a crucial role in its interaction with positively charged macromolecules and ions. Among these macromolecules, positively charged arginine molecules or polyarginine peptides demonstrate potential in drug delivery when complexed with hyaluronan. This study aimed to compare and elucidate the results of both experimental and computational investigations on the interactions between hyaluronic acid polymers and polyarginine peptides. Experimental findings revealed that by varying the length of polyarginine peptides and the molar ratio, it is possible to modulate the size, solubility, and stability of hyaluronan-arginine particles. To further explore these interactions, molecular dynamics simulations were conducted to model the complexes formed between hyaluronic acid polymers and arginine peptides. The simulations are considered in different molar ratios and lengths of polyarginine peptides. By analysis of the data, we successfully determined the shape and size of the resulting complexes. Additionally, we identified the primary driving forces behind complex formation and explained the observed variations in peptide interactions with hyaluronan 
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700 1 |a Minofar, Babak  |e verfasserin  |4 aut 
700 1 |a Jugl, Adam  |e verfasserin  |4 aut 
700 1 |a Pekař, Miloslav  |e verfasserin  |4 aut 
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