Interactions of A1(III) with phosphorylated amino acids

Erzsébet Kiss, A. Lakatos, I. Bányai, T. Kiss

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

In order to assess the A1(III)-binding abilities of phosphorylated proteins and peptides, the interactions of A1(III) with the building blocks O-phosphoserine (PSer) and O-phosphotyrosine (PTyr) were studied. pH-metric and 31P NMR measurements were carried out to determine the stoichiometries and stability constants of the complexes formed, and to establish the most probable binding sites of the metal ion. PSer was found to bind A1(III) in a monodentate manner at the phosphate moiety, and in a tridentate manner with the simultaneous coordination of all donor groups. PTyr binds A1(III) only at the separate phosphate function. Citric acid (Cit) proved to be a stronger A1(III) binder at the physiological pH, though, it was able to displace PSer only in a rather slow process through formation of the trinuclear species A13(Cit)3(OH). The results were used to evaluate the potential role of A1(III) in inducing the formation of neurofilamentous aggregates in neurological disorders.

Original languageEnglish
Pages (from-to)145-151
Number of pages7
JournalJournal of Inorganic Biochemistry
Volume69
Issue number3
DOIs
Publication statusPublished - Feb 15 1998

Fingerprint

Phosphoserine
Phosphotyrosine
Amino Acids
Citric Acid
Phosphates
Nervous System Diseases
Stoichiometry
Binders
Metal ions
Metals
Binding Sites
Nuclear magnetic resonance
Ions
Peptides
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

Interactions of A1(III) with phosphorylated amino acids. / Kiss, Erzsébet; Lakatos, A.; Bányai, I.; Kiss, T.

In: Journal of Inorganic Biochemistry, Vol. 69, No. 3, 15.02.1998, p. 145-151.

Research output: Contribution to journalArticle

@article{794315a4ead04de7a19898daab74d410,
title = "Interactions of A1(III) with phosphorylated amino acids",
abstract = "In order to assess the A1(III)-binding abilities of phosphorylated proteins and peptides, the interactions of A1(III) with the building blocks O-phosphoserine (PSer) and O-phosphotyrosine (PTyr) were studied. pH-metric and 31P NMR measurements were carried out to determine the stoichiometries and stability constants of the complexes formed, and to establish the most probable binding sites of the metal ion. PSer was found to bind A1(III) in a monodentate manner at the phosphate moiety, and in a tridentate manner with the simultaneous coordination of all donor groups. PTyr binds A1(III) only at the separate phosphate function. Citric acid (Cit) proved to be a stronger A1(III) binder at the physiological pH, though, it was able to displace PSer only in a rather slow process through formation of the trinuclear species A13(Cit)3(OH). The results were used to evaluate the potential role of A1(III) in inducing the formation of neurofilamentous aggregates in neurological disorders.",
author = "Erzs{\'e}bet Kiss and A. Lakatos and I. B{\'a}nyai and T. Kiss",
year = "1998",
month = "2",
day = "15",
doi = "10.1016/S0162-0134(97)10011-3",
language = "English",
volume = "69",
pages = "145--151",
journal = "Journal of Inorganic Biochemistry",
issn = "0162-0134",
publisher = "Elsevier Inc.",
number = "3",

}

TY - JOUR

T1 - Interactions of A1(III) with phosphorylated amino acids

AU - Kiss, Erzsébet

AU - Lakatos, A.

AU - Bányai, I.

AU - Kiss, T.

PY - 1998/2/15

Y1 - 1998/2/15

N2 - In order to assess the A1(III)-binding abilities of phosphorylated proteins and peptides, the interactions of A1(III) with the building blocks O-phosphoserine (PSer) and O-phosphotyrosine (PTyr) were studied. pH-metric and 31P NMR measurements were carried out to determine the stoichiometries and stability constants of the complexes formed, and to establish the most probable binding sites of the metal ion. PSer was found to bind A1(III) in a monodentate manner at the phosphate moiety, and in a tridentate manner with the simultaneous coordination of all donor groups. PTyr binds A1(III) only at the separate phosphate function. Citric acid (Cit) proved to be a stronger A1(III) binder at the physiological pH, though, it was able to displace PSer only in a rather slow process through formation of the trinuclear species A13(Cit)3(OH). The results were used to evaluate the potential role of A1(III) in inducing the formation of neurofilamentous aggregates in neurological disorders.

AB - In order to assess the A1(III)-binding abilities of phosphorylated proteins and peptides, the interactions of A1(III) with the building blocks O-phosphoserine (PSer) and O-phosphotyrosine (PTyr) were studied. pH-metric and 31P NMR measurements were carried out to determine the stoichiometries and stability constants of the complexes formed, and to establish the most probable binding sites of the metal ion. PSer was found to bind A1(III) in a monodentate manner at the phosphate moiety, and in a tridentate manner with the simultaneous coordination of all donor groups. PTyr binds A1(III) only at the separate phosphate function. Citric acid (Cit) proved to be a stronger A1(III) binder at the physiological pH, though, it was able to displace PSer only in a rather slow process through formation of the trinuclear species A13(Cit)3(OH). The results were used to evaluate the potential role of A1(III) in inducing the formation of neurofilamentous aggregates in neurological disorders.

UR - http://www.scopus.com/inward/record.url?scp=0031864147&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031864147&partnerID=8YFLogxK

U2 - 10.1016/S0162-0134(97)10011-3

DO - 10.1016/S0162-0134(97)10011-3

M3 - Article

VL - 69

SP - 145

EP - 151

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

SN - 0162-0134

IS - 3

ER -