Hyaluronan-cecropin B interactions studied by ultrasound velocimetry and isothermal titration calorimetry

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216305%3A26310%2F23%3APU146631" target="_blank" >RIV/00216305:26310/23:PU146631 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S014181302203046X?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S014181302203046X?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.ijbiomac.2022.12.144" target="_blank" >10.1016/j.ijbiomac.2022.12.144</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Hyaluronan-cecropin B interactions studied by ultrasound velocimetry and isothermal titration calorimetry

Popis výsledku v původním jazyce

Interactions between hyaluronan and the antimicrobial peptide cecropin B were studied in water and PBS using high-resolution ultrasonic spectroscopy and isothermal titration calorimetry. Although each technique is fundamentally different, they both gave identical results. It was found that the molecular weight of hyaluronan plays an important role in the interactions - in particular, the transition between the rod conformation and the random coil conformation. In water, interactions were saturated in a molar charge ratio of 1.5 and not 1.0 as expected. The later saturation of the interaction probably occurred either for steric reasons or due to the interaction between functional groups in the cecropin structure, which allowed complete dissociation of the antimicrobial peptide. In PBS, in contrast to water, no interactions were observed, irrespective of the molecular weight of hyaluronan. Thus, at a sufficiently high ionic strength, the interactions were suppressed.

Název v anglickém jazyce

Hyaluronan-cecropin B interactions studied by ultrasound velocimetry and isothermal titration calorimetry

Popis výsledku anglicky

Interactions between hyaluronan and the antimicrobial peptide cecropin B were studied in water and PBS using high-resolution ultrasonic spectroscopy and isothermal titration calorimetry. Although each technique is fundamentally different, they both gave identical results. It was found that the molecular weight of hyaluronan plays an important role in the interactions - in particular, the transition between the rod conformation and the random coil conformation. In water, interactions were saturated in a molar charge ratio of 1.5 and not 1.0 as expected. The later saturation of the interaction probably occurred either for steric reasons or due to the interaction between functional groups in the cecropin structure, which allowed complete dissociation of the antimicrobial peptide. In PBS, in contrast to water, no interactions were observed, irrespective of the molecular weight of hyaluronan. Thus, at a sufficiently high ionic strength, the interactions were suppressed.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

—

Návaznosti

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2023

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

ISSN

0141-8130

e-ISSN

1879-0003

Svazek periodika

227

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

786-794

Kód UT WoS článku

000909884500001

EID výsledku v databázi Scopus

2-s2.0-85144540297