Computational Study of Complex Formation between Hyaluronan Polymers and Polyarginine Peptides at Various Ratios
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F23%3A00578099" target="_blank" >RIV/61388971:_____/23:00578099 - isvavai.cz</a>
Alternative codes found
RIV/60076658:12310/23:43907305 RIV/00216305:26310/23:PU149227
Result on the web
<a href="https://pubs.acs.org/doi/10.1021/acs.langmuir.3c01318" target="_blank" >https://pubs.acs.org/doi/10.1021/acs.langmuir.3c01318</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.langmuir.3c01318" target="_blank" >10.1021/acs.langmuir.3c01318</a>
Alternative languages
Result language
angličtina
Original language name
Computational Study of Complex Formation between Hyaluronan Polymers and Polyarginine Peptides at Various Ratios
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10403 - Physical chemistry
Result continuities
Project
—
Continuities
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Others
Publication year
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Langmuir
ISSN
0743-7463
e-ISSN
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Volume of the periodical
39
Issue of the periodical within the volume
40
Country of publishing house
US - UNITED STATES
Number of pages
11
Pages from-to
14212-14222
UT code for WoS article
001076097500001
EID of the result in the Scopus database
2-s2.0-85173588778