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
Chiral CE methods were developed for the elucidation of l‐ or d‐configuration of tyrosine residue in antimicrobial dipeptide β‐alanyl‐tyrosine (β‐Ala‐Tyr) isolated from the hemolymph of larvae of fleshfly Neobellieria bullata and for the evaluation of enantiopurity of its synthetic isomers (β‐Ala‐d‐...
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| Published in | Journal of separation science Vol. 45; no. 17; pp. 3328 - 3338 |
|---|---|
| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Germany
Wiley Subscription Services, Inc
01.09.2022
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| Subjects | |
| Online Access | Get full text |
| ISSN | 1615-9306 1615-9314 1615-9314 |
| DOI | 10.1002/jssc.202200158 |
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| Abstract | Chiral CE methods were developed for the elucidation of l‐ or d‐configuration of tyrosine residue in antimicrobial dipeptide β‐alanyl‐tyrosine (β‐Ala‐Tyr) isolated from the hemolymph of larvae of fleshfly Neobellieria bullata and for the evaluation of enantiopurity of its synthetic isomers (β‐Ala‐d‐Tyr and β‐Ala‐l‐Tyr), and enantiomers of their amidated and acetylated derivatives, β‐Ala‐d,l‐Tyr‐NH2 and N‐Ac‐β‐Ala‐d,l‐Tyr, respectively. Baseline separations were achieved for all three pairs of enantiomers: (i) for β‐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‐β‐cyclodextrin as chiral selector; (ii) for β‐Ala‐d,l‐Tyr‐NH2 enantiomers in acidic background electrolyte consisting of 48/50 mM tris(hydroxymethyl)aminomethane/H3PO4, pH 3.5, and 30 mg/mL 2‐hydroxypropyl‐β‐cyclodextrin; and (iii) for enantiomers of N‐Ac‐β‐Ala‐d,l‐Tyr in alkaline background electrolyte composed of 50/49 mM Na2B4O7/NaOH, pH 10.5, and 60 mg/mL 2‐hydroxypropyl‐β‐cyclodextrin. From CE analyses of mixed samples of isolated β‐Ala‐Tyr and synthetic standards β‐Ala‐l‐Tyr and β‐Ala‐d‐Tyr, it turned out that isolated β‐Ala‐Tyr was pure l‐enantiomer. In addition, the average apparent binding constants, Kb, and average actual ionic mobilities of the complexes of β‐Ala‐d,l‐Tyr and its above derivatives with 2‐hydroxypropyl‐β‐cyclodextrin were determined. These complexes were weak, with Kb values ranging from 11.2 to 79.1 L/mol. Their cationic mobilities were equal to (5.6–9.2) × 10–9 m2/V/s, and anionic mobilities to (‐1.3–1.6) × 10–9 m2/V/s. |
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| AbstractList | Chiral CE methods were developed for the elucidation of
l
‐ or
d
‐configuration of tyrosine residue in antimicrobial dipeptide β‐alanyl‐tyrosine (β‐Ala‐Tyr) isolated from the hemolymph of larvae of fleshfly
Neobellieria bullata
and for the evaluation of enantiopurity of its synthetic isomers (β
‐
Ala
‐d‐
Tyr and β
‐
Ala‐
l
‐Tyr), and enantiomers of their amidated and acetylated derivatives, β‐Ala‐
d
,
l
‐Tyr‐NH
2
and
N
‐Ac‐β‐Ala‐
d
,
l
‐Tyr, respectively. Baseline separations were achieved for all three pairs of enantiomers: (i) for β‐Ala‐
d
,
l
‐Tyr in acidic background electrolyte composed of 32/50 mM tris(hydroxymethyl)aminomethane/H
3
PO
4
, pH 2.5, and 20 mg/mL 2‐hydroxypropyl‐β‐cyclodextrin as chiral selector; (ii) for β‐Ala‐
d,l
‐Tyr‐NH
2
enantiomers in acidic background electrolyte consisting of 48/50 mM tris(hydroxymethyl)aminomethane/H
3
PO
4
, pH 3.5, and 30 mg/mL 2‐hydroxypropyl‐β‐cyclodextrin; and (iii) for enantiomers of
N
‐Ac‐β‐Ala‐
d
,
l
‐Tyr in alkaline background electrolyte composed of 50/49 mM Na
2
B
4
O
7
/NaOH, pH 10.5, and 60 mg/mL 2‐hydroxypropyl‐β‐cyclodextrin. From CE analyses of mixed samples of isolated β‐Ala‐Tyr and synthetic standards β‐Ala‐
l
‐Tyr and β‐Ala‐
d
‐Tyr, it turned out that isolated β‐Ala‐Tyr was pure
l
‐enantiomer. In addition, the average apparent binding constants,
K
b
, and average actual ionic mobilities of the complexes of β‐Ala‐
d
,
l
‐Tyr and its above derivatives with 2‐hydroxypropyl‐β‐cyclodextrin 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) × 10
–9
m
2
/V/s, and anionic mobilities to (‐1.3–1.6) × 10
–9
m
2
/V/s. Chiral CE methods were developed for the elucidation of l- or d-configuration of tyrosine residue in antimicrobial dipeptide β-alanyl-tyrosine (β-Ala-Tyr) isolated from the hemolymph of larvae of fleshfly Neobellieria bullata and for the evaluation of enantiopurity of its synthetic isomers (β-Ala-d-Tyr and β-Ala-l-Tyr), and enantiomers of their amidated and acetylated derivatives, β-Ala-d,l-Tyr-NH2 and N-Ac-β-Ala-d,l-Tyr, respectively. Baseline separations were achieved for all three pairs of enantiomers: (i) for β-Ala-d,l-Tyr in acidic background electrolyte composed of 32/50 mM tris(hydroxymethyl)aminomethane/H3 PO4 , pH 2.5, and 20 mg/mL 2-hydroxypropyl-β-cyclodextrin as chiral selector; (ii) for β-Ala-d,l-Tyr-NH2 enantiomers in acidic background electrolyte consisting of 48/50 mM tris(hydroxymethyl)aminomethane/H3 PO4 , pH 3.5, and 30 mg/mL 2-hydroxypropyl-β-cyclodextrin; and (iii) for enantiomers of N-Ac-β-Ala-d,l-Tyr in alkaline background electrolyte composed of 50/49 mM Na2 B4 O7 /NaOH, pH 10.5, and 60 mg/mL 2-hydroxypropyl-β-cyclodextrin. From CE analyses of mixed samples of isolated β-Ala-Tyr and synthetic standards β-Ala-l-Tyr and β-Ala-d-Tyr, it turned out that isolated β-Ala-Tyr was pure l-enantiomer. In addition, the average apparent binding constants, Kb , and average actual ionic mobilities of the complexes of β-Ala-d,l-Tyr and its above derivatives with 2-hydroxypropyl-β-cyclodextrin were determined. These complexes were weak, with Kb values ranging from 11.2 to 79.1 L/mol. Their cationic mobilities were equal to (5.6-9.2) × 10-9 m2 /V/s, and anionic mobilities to (-1.3-1.6) × 10-9 m2 /V/s.Chiral CE methods were developed for the elucidation of l- or d-configuration of tyrosine residue in antimicrobial dipeptide β-alanyl-tyrosine (β-Ala-Tyr) isolated from the hemolymph of larvae of fleshfly Neobellieria bullata and for the evaluation of enantiopurity of its synthetic isomers (β-Ala-d-Tyr and β-Ala-l-Tyr), and enantiomers of their amidated and acetylated derivatives, β-Ala-d,l-Tyr-NH2 and N-Ac-β-Ala-d,l-Tyr, respectively. Baseline separations were achieved for all three pairs of enantiomers: (i) for β-Ala-d,l-Tyr in acidic background electrolyte composed of 32/50 mM tris(hydroxymethyl)aminomethane/H3 PO4 , pH 2.5, and 20 mg/mL 2-hydroxypropyl-β-cyclodextrin as chiral selector; (ii) for β-Ala-d,l-Tyr-NH2 enantiomers in acidic background electrolyte consisting of 48/50 mM tris(hydroxymethyl)aminomethane/H3 PO4 , pH 3.5, and 30 mg/mL 2-hydroxypropyl-β-cyclodextrin; and (iii) for enantiomers of N-Ac-β-Ala-d,l-Tyr in alkaline background electrolyte composed of 50/49 mM Na2 B4 O7 /NaOH, pH 10.5, and 60 mg/mL 2-hydroxypropyl-β-cyclodextrin. From CE analyses of mixed samples of isolated β-Ala-Tyr and synthetic standards β-Ala-l-Tyr and β-Ala-d-Tyr, it turned out that isolated β-Ala-Tyr was pure l-enantiomer. In addition, the average apparent binding constants, Kb , and average actual ionic mobilities of the complexes of β-Ala-d,l-Tyr and its above derivatives with 2-hydroxypropyl-β-cyclodextrin were determined. These complexes were weak, with Kb values ranging from 11.2 to 79.1 L/mol. Their cationic mobilities were equal to (5.6-9.2) × 10-9 m2 /V/s, and anionic mobilities to (-1.3-1.6) × 10-9 m2 /V/s. Chiral CE methods were developed for the elucidation of l‐ or d‐configuration of tyrosine residue in antimicrobial dipeptide β‐alanyl‐tyrosine (β‐Ala‐Tyr) isolated from the hemolymph of larvae of fleshfly Neobellieria bullata and for the evaluation of enantiopurity of its synthetic isomers (β‐Ala‐d‐Tyr and β‐Ala‐l‐Tyr), and enantiomers of their amidated and acetylated derivatives, β‐Ala‐d,l‐Tyr‐NH2 and N‐Ac‐β‐Ala‐d,l‐Tyr, respectively. Baseline separations were achieved for all three pairs of enantiomers: (i) for β‐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‐β‐cyclodextrin as chiral selector; (ii) for β‐Ala‐d,l‐Tyr‐NH2 enantiomers in acidic background electrolyte consisting of 48/50 mM tris(hydroxymethyl)aminomethane/H3PO4, pH 3.5, and 30 mg/mL 2‐hydroxypropyl‐β‐cyclodextrin; and (iii) for enantiomers of N‐Ac‐β‐Ala‐d,l‐Tyr in alkaline background electrolyte composed of 50/49 mM Na2B4O7/NaOH, pH 10.5, and 60 mg/mL 2‐hydroxypropyl‐β‐cyclodextrin. From CE analyses of mixed samples of isolated β‐Ala‐Tyr and synthetic standards β‐Ala‐l‐Tyr and β‐Ala‐d‐Tyr, it turned out that isolated β‐Ala‐Tyr was pure l‐enantiomer. In addition, the average apparent binding constants, Kb, and average actual ionic mobilities of the complexes of β‐Ala‐d,l‐Tyr and its above derivatives with 2‐hydroxypropyl‐β‐cyclodextrin were determined. These complexes were weak, with Kb values ranging from 11.2 to 79.1 L/mol. Their cationic mobilities were equal to (5.6–9.2) × 10–9 m2/V/s, and anionic mobilities to (‐1.3–1.6) × 10–9 m2/V/s. Chiral CE methods were developed for the elucidation of l- or d-configuration of tyrosine residue in antimicrobial dipeptide β-alanyl-tyrosine (β-Ala-Tyr) isolated from the hemolymph of larvae of fleshfly Neobellieria bullata and for the evaluation of enantiopurity of its synthetic isomers (β-Ala-d-Tyr and β-Ala-l-Tyr), and enantiomers of their amidated and acetylated derivatives, β-Ala-d,l-Tyr-NH and N-Ac-β-Ala-d,l-Tyr, respectively. Baseline separations were achieved for all three pairs of enantiomers: (i) for β-Ala-d,l-Tyr in acidic background electrolyte composed of 32/50 mM tris(hydroxymethyl)aminomethane/H PO , pH 2.5, and 20 mg/mL 2-hydroxypropyl-β-cyclodextrin as chiral selector; (ii) for β-Ala-d,l-Tyr-NH enantiomers in acidic background electrolyte consisting of 48/50 mM tris(hydroxymethyl)aminomethane/H PO , pH 3.5, and 30 mg/mL 2-hydroxypropyl-β-cyclodextrin; and (iii) for enantiomers of N-Ac-β-Ala-d,l-Tyr in alkaline background electrolyte composed of 50/49 mM Na B O /NaOH, pH 10.5, and 60 mg/mL 2-hydroxypropyl-β-cyclodextrin. From CE analyses of mixed samples of isolated β-Ala-Tyr and synthetic standards β-Ala-l-Tyr and β-Ala-d-Tyr, it turned out that isolated β-Ala-Tyr was pure l-enantiomer. In addition, the average apparent binding constants, K , and average actual ionic mobilities of the complexes of β-Ala-d,l-Tyr and its above derivatives with 2-hydroxypropyl-β-cyclodextrin were determined. These complexes were weak, with K values ranging from 11.2 to 79.1 L/mol. Their cationic mobilities were equal to (5.6-9.2) × 10 m /V/s, and anionic mobilities to (-1.3-1.6) × 10 m /V/s. Chiral CE methods were developed for the elucidation of l‐ or d‐configuration of tyrosine residue in antimicrobial dipeptide β‐alanyl‐tyrosine (β‐Ala‐Tyr) isolated from the hemolymph of larvae of fleshfly Neobellieria bullata and for the evaluation of enantiopurity of its synthetic isomers (β‐Ala‐d‐Tyr and β‐Ala‐l‐Tyr), and enantiomers of their amidated and acetylated derivatives, β‐Ala‐d,l‐Tyr‐NH₂ and N‐Ac‐β‐Ala‐d,l‐Tyr, respectively. Baseline separations were achieved for all three pairs of enantiomers: (i) for β‐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‐β‐cyclodextrin as chiral selector; (ii) for β‐Ala‐d,l‐Tyr‐NH₂ enantiomers in acidic background electrolyte consisting of 48/50 mM tris(hydroxymethyl)aminomethane/H₃PO₄, pH 3.5, and 30 mg/mL 2‐hydroxypropyl‐β‐cyclodextrin; and (iii) for enantiomers of N‐Ac‐β‐Ala‐d,l‐Tyr in alkaline background electrolyte composed of 50/49 mM Na₂B₄O₇/NaOH, pH 10.5, and 60 mg/mL 2‐hydroxypropyl‐β‐cyclodextrin. From CE analyses of mixed samples of isolated β‐Ala‐Tyr and synthetic standards β‐Ala‐l‐Tyr and β‐Ala‐d‐Tyr, it turned out that isolated β‐Ala‐Tyr was pure l‐enantiomer. In addition, the average apparent binding constants, Kb, and average actual ionic mobilities of the complexes of β‐Ala‐d,l‐Tyr and its above derivatives with 2‐hydroxypropyl‐β‐cyclodextrin were determined. These complexes were weak, with Kb values ranging from 11.2 to 79.1 L/mol. Their cationic mobilities were equal to (5.6–9.2) × 10–⁹ m²/V/s, and anionic mobilities to (‐1.3–1.6) × 10–⁹ m²/V/s. Chiral CE methods were developed for the elucidation of l‐ or d‐configuration of tyrosine residue in antimicrobial dipeptide β‐alanyl‐tyrosine (β‐Ala‐Tyr) isolated from the hemolymph of larvae of fleshfly Neobellieria bullata and for the evaluation of enantiopurity of its synthetic isomers (β‐Ala‐d‐Tyr and β‐Ala‐l‐Tyr), and enantiomers of their amidated and acetylated derivatives, β‐Ala‐d,l‐Tyr‐NH2 and N‐Ac‐β‐Ala‐d,l‐Tyr, respectively. Baseline separations were achieved for all three pairs of enantiomers: (i) for β‐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‐β‐cyclodextrin as chiral selector; (ii) for β‐Ala‐d,l‐Tyr‐NH2 enantiomers in acidic background electrolyte consisting of 48/50 mM tris(hydroxymethyl)aminomethane/H3PO4, pH 3.5, and 30 mg/mL 2‐hydroxypropyl‐β‐cyclodextrin; and (iii) for enantiomers of N‐Ac‐β‐Ala‐d,l‐Tyr in alkaline background electrolyte composed of 50/49 mM Na2B4O7/NaOH, pH 10.5, and 60 mg/mL 2‐hydroxypropyl‐β‐cyclodextrin. From CE analyses of mixed samples of isolated β‐Ala‐Tyr and synthetic standards β‐Ala‐l‐Tyr and β‐Ala‐d‐Tyr, it turned out that isolated β‐Ala‐Tyr was pure l‐enantiomer. In addition, the average apparent binding constants, Kb, and average actual ionic mobilities of the complexes of β‐Ala‐d,l‐Tyr and its above derivatives with 2‐hydroxypropyl‐β‐cyclodextrin were determined. These complexes were weak, with Kb values ranging from 11.2 to 79.1 L/mol. Their cationic mobilities were equal to (5.6–9.2) × 10–9 m2/V/s, and anionic mobilities to (‐1.3–1.6) × 10–9 m2/V/s. |
| Author | Schimperková, Tereza Jiráček, Jiří Šolínová, Veronika Kašička, Václav Sázelová, Petra |
| Author_xml | – sequence: 1 givenname: Petra surname: Sázelová fullname: Sázelová, Petra organization: Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences – sequence: 2 givenname: Veronika surname: Šolínová fullname: Šolínová, Veronika organization: Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences – sequence: 3 givenname: Tereza surname: Schimperková fullname: Schimperková, Tereza organization: Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences – sequence: 4 givenname: Jiří surname: Jiráček fullname: Jiráček, Jiří organization: Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences – sequence: 5 givenname: Václav orcidid: 0000-0003-1719-1432 surname: Kašička fullname: Kašička, Václav email: kasicka@uochb.cas.cz organization: Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/35462458$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1002_jssc_202400352 crossref_primary_10_1016_j_talanta_2025_128004 crossref_primary_10_1002_jssc_70043 crossref_primary_10_1039_D2AY02111K crossref_primary_10_1002_elps_202300152 crossref_primary_10_1002_jssc_202400174 crossref_primary_10_1002_elps_202200279 crossref_primary_10_1016_j_chroma_2023_464214 crossref_primary_10_1002_jssc_202200453 |
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| Keywords | enantioseparation 2-hydroxypropyl-β-cyclodextrin chiral separation capillary electrophoresis Binding constant β-alanyl-tyrosine |
| Language | English |
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| Snippet | Chiral CE methods were developed for the elucidation of l‐ or d‐configuration of tyrosine residue in antimicrobial dipeptide β‐alanyl‐tyrosine (β‐Ala‐Tyr)... Chiral CE methods were developed for the elucidation of l ‐ or d ‐configuration of tyrosine residue in antimicrobial dipeptide β‐alanyl‐tyrosine (β‐Ala‐Tyr)... Chiral CE methods were developed for the elucidation of l- or d-configuration of tyrosine residue in antimicrobial dipeptide β-alanyl-tyrosine (β-Ala-Tyr)... |
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| SubjectTerms | 2‐hydroxypropyl‐β‐cyclodextrin Antiinfectives and antibacterials Binding Binding constant capillary electrophoresis chiral separation Cyclodextrins dipeptides Electrolytes Electrophoresis Enantiomers enantioseparation hemolymph Larvae Sarcophaga bullata separation Tyrosine β‐alanyl‐tyrosine |
| Title | 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 |
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