2008
CE study of neuroprotective humanin peptide and its derivatives: Interactions with phosphate, sulphate, alkylsulphonates and sulphated-beta-CD
HAVEL, Josef; Rong LI a Mirek MACKAZákladní údaje
Originální název
CE study of neuroprotective humanin peptide and its derivatives: Interactions with phosphate, sulphate, alkylsulphonates and sulphated-beta-CD
Autoři
HAVEL, Josef; Rong LI a Mirek MACKA
Vydání
Electrophoresis, HOBOKEN, Verlag Chemie, 2008, 0173-0835
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10406 Analytical chemistry
Stát vydavatele
Německo
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 3.509
Označené pro přenos do RIV
Ano
Organizační jednotka
Přírodovědecká fakulta
UT WoS
EID Scopus
Klíčová slova anglicky
CE; humanin peptide derivatives; interaction; ion associates; sulphated-beta-CD
Štítky
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 30. 6. 2020 09:45, Mgr. Marie Novosadová Šípková, DiS.
Anotace
V originále
Humanin (HN), Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-IIe-Asp-Leu- Pro-Val-Lys-Arg-Arg-Ala, recently discovered in the human brain, is an important neuroprotective peptide. Some derivatives of HN show even higher biological activity, for example [G-14]-HN, where Ser at position 14 is replaced with Gly. As structurally related HN peptide derivatives have similar chemical properties, their separation by CE is difficult. In this work, the electrophoretic behaviour of HN derivatives including [G-14]-HN, a tryptophan HN derivative [W-14]-HN, several other HN derivatives and HN fragments was studied. While phosphate buffer was used as the general BGE, the effects of the buffer concentration and various additives were examined, including sulphate, heptane sulphonate, 2-morpholinoethanesulphonic acid N-[tris(hydroxymethyl)methyl]-2-amino-ethane sulphonic acid (TES), sulphated-beta-CD and beta-CD. Separation efficiency of 200 000 theoretical plates was achieved in a BGE of 80 mM phosphate at pH 2.5 where seven out of nine major peaks were partially separated. By investigating the influence of concentration of the interrogated ions on peptides migration, the association between positively charged protonated sites of peptides and various anions was proved. Especially a strong interaction with phosphate, sulphate and sulphonate groups was established. Conditional stability constant of the [Pep(z+), (H2PO4-)(n)](z-n) ion associate (n = 1) for [G-14]-HN equals to log K similar to 1.78.
Návaznosti
| GA305/03/1100, projekt VaV |
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| LC06035, projekt VaV |
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