Chiral analysis of β-alanyl-D,L-tyrosine and its derivatives and estimation of binding constants of their complexes with 2-hydroxypropyl-β-cyclodextrin by capillary electrophoresis

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F22%3A00557298" target="_blank" >RIV/61388963:_____/22:00557298 - isvavai.cz</a>

Výsledek na webu

<a href="https://doi.org/10.1002/jssc.202200158" target="_blank" >https://doi.org/10.1002/jssc.202200158</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/jssc.202200158" target="_blank" >10.1002/jssc.202200158</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Chiral analysis of β-alanyl-D,L-tyrosine and its derivatives and estimation of binding constants of their complexes with 2-hydroxypropyl-β-cyclodextrin by capillary electrophoresis

Popis výsledku v původním jazyce

Chiral CE methods were developed for the elucidation of L- or D-configuration of tyrosine residue in antimicrobial dipeptide beta-alanyl-tyrosine (beta-Ala-Tyr) isolated from the hemolymph of larvae of fleshfly Neobellieria bullata and for the evaluation of enantiopurity of its synthetic isomers (beta-Ala-D-Tyr and beta-Ala-L-Tyr), and enantiomers of their amidated and acetylated derivatives, beta-Ala-D,L-Tyr-NH2 and N-Ac-beta-Ala-D,L-Tyr, respectively. Baseline separations were achieved for all three pairs of enantiomers: (i) for beta-Ala-D,L-Tyr in acidic background electrolyte composed of 32/50 mM tris(hydroxymethyl)aminomethane/H3PO4, pH 2.5, and 20 mg/mL 2-hydroxypropyl-beta-cyclodextrin as chiral selector, (ii) for beta-Ala-D,L-Tyr-NH, enantiomers in acidic background electrolyte consisting of 48/50 mM tris(hydroxymethyl)aminomethane/H3PO4, pH 3.5, and 30 mg/mL 2-hydroxypropyl-beta-cyclodextrin, and (iii) for enantiomers of N-Ac-beta-Ala-D,L-Tyr in alkaline background electrolyte composed of 50/49 mM Na2B4O7/NaOH, pH 10.5, and 60 mg/mL 2-hydroxypropyl-beta-cyclodextrin. From CE analyses of mixed samples of isolated beta-Ala-Tyr and synthetic standards beta-Ala-L-Tyr and beta-Ala-DTyr, it turned out that isolated beta-Ala-Tyr was pure L-enantiomer. In addition, the average apparent binding constants, K-b, and average actual ionic mobilities of the complexes of beta-Ala-D,L-Tyr and its above derivatives with 2-hydroxypropyl-Acyclodextrin were determined. These complexes were weak, with K-b values ranging from 11.2 to 79.1 L/mol. Their cationic mobilities were equal to (5.6-9.2) x 10(-9) m(2)/V/s, and anionic mobilities to (-1.3-1.6) x 10(-9) m(2)/V/s.

Název v anglickém jazyce

Chiral analysis of β-alanyl-D,L-tyrosine and its derivatives and estimation of binding constants of their complexes with 2-hydroxypropyl-β-cyclodextrin by capillary electrophoresis

Popis výsledku anglicky

Chiral CE methods were developed for the elucidation of L- or D-configuration of tyrosine residue in antimicrobial dipeptide beta-alanyl-tyrosine (beta-Ala-Tyr) isolated from the hemolymph of larvae of fleshfly Neobellieria bullata and for the evaluation of enantiopurity of its synthetic isomers (beta-Ala-D-Tyr and beta-Ala-L-Tyr), and enantiomers of their amidated and acetylated derivatives, beta-Ala-D,L-Tyr-NH2 and N-Ac-beta-Ala-D,L-Tyr, respectively. Baseline separations were achieved for all three pairs of enantiomers: (i) for beta-Ala-D,L-Tyr in acidic background electrolyte composed of 32/50 mM tris(hydroxymethyl)aminomethane/H3PO4, pH 2.5, and 20 mg/mL 2-hydroxypropyl-beta-cyclodextrin as chiral selector, (ii) for beta-Ala-D,L-Tyr-NH, enantiomers in acidic background electrolyte consisting of 48/50 mM tris(hydroxymethyl)aminomethane/H3PO4, pH 3.5, and 30 mg/mL 2-hydroxypropyl-beta-cyclodextrin, and (iii) for enantiomers of N-Ac-beta-Ala-D,L-Tyr in alkaline background electrolyte composed of 50/49 mM Na2B4O7/NaOH, pH 10.5, and 60 mg/mL 2-hydroxypropyl-beta-cyclodextrin. From CE analyses of mixed samples of isolated beta-Ala-Tyr and synthetic standards beta-Ala-L-Tyr and beta-Ala-DTyr, it turned out that isolated beta-Ala-Tyr was pure L-enantiomer. In addition, the average apparent binding constants, K-b, and average actual ionic mobilities of the complexes of beta-Ala-D,L-Tyr and its above derivatives with 2-hydroxypropyl-Acyclodextrin were determined. These complexes were weak, with K-b values ranging from 11.2 to 79.1 L/mol. Their cationic mobilities were equal to (5.6-9.2) x 10(-9) m(2)/V/s, and anionic mobilities to (-1.3-1.6) x 10(-9) m(2)/V/s.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10406 - Analytical chemistry

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2022

Kód důvěrnosti údajů

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

Název periodika

Journal of Separation Science

ISSN

1615-9306

e-ISSN

1615-9314

Svazek periodika

45

Číslo periodika v rámci svazku

17

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

11

Strana od-do

3328-3338

Kód UT WoS článku

000790115700001

EID výsledku v databázi Scopus

2-s2.0-85129563676