Complexes of aluminium with peptide ligands: A fourier transform IR spectroscopic study

抄録

<jats:title>Abstract</jats:title><jats:p>Aluminium has been recognized to be a neurotoxic agent and a risk factor in Alzheimer's disease and other neuronal dysfunctions. CD spectroscopic studies on two synthetic fragments of the human neurofilament protein midsized subunit (NF‐M), and their alanine‐for‐serine‐substituled and /or serine‐phosphorylated derivatives showed the formation of stable, citric acid resistant complexes of Al<jats:sup>3+</jats:sup>with peptide ligands [M. Hollósi, Z.M. Shen, A. Perczel, and G.D. Fasman (1994) Proc. Natl. Acad. Sci. USA, vol. <jats:bold>9</jats:bold>, pp.4902‐4906]. In the case of Ser‐phosphorylated fragments, aβ‐sheet inducing effect of Ca<jats:sup>2+</jats:sup> and Al<jats:sup>3+</jats:sup> ions was observed. However, the serine‐containing parent peptides, NF‐M 13 (KSPVPKSPVEEKG) and NF‐M 17 (EEKGKSPVPKSPVEEKG), failed to show CD spectral changes reflecting β‐sheet formation upon addition of Al<jats:sup>3+</jats:sup> ions. On the basis of the amide I region of the Fourier transform ir spectra, in triftuoroethanol, the peptide backbone of NF‐M17 and NF‐M17 (A<jats:sup>6</jats:sup>A<jats:sup>11</jats:sup>) shows marked changes in the presence ofAl<jats:sup>3+</jats:sup>. The most significant spectral differences are seen in the car‐boxyl region (> 1700 cm<jats:sup>−l</jats:sup>). The high‐frequency component bands above 1760 cm<jats:sup>−1</jats:sup> in both spectra belong to the C O of undissociated CF<jats:sub>3</jats:sub>COOH. Another strong band at 1710 cm<jats:sup>−1</jats:sup> which appears only in the spectrum of NF‐Ml 7 (A<jats:sup>6</jats:sup>A<jats:sup>11</jats:sup>)(NF‐M17 with Ser<jats:sup>6</jats:sup> andSer<jats:sup>11</jats:sup> replaced by Ala) can be assigned to the side chain or C‐terminal COOH groups. The differential proton‐ation state of the carboxyl groups in the two peptides suggests the format ion ofAl<jats:sup>3+</jats:sup> complexes of different structure and stability. The Al<jats:sup>3+</jats:sup> complex ofNF‐Ml 7 (A<jats:sup>6</jats:sup>A<jats:sup>11</jats:sup>) is likely less stable, or one or more of the carboxylates are not coordinated to the Al<jats:sup>3+</jats:sup> and thus can serve as a base to bind the liberated protons. In NF‐M17 the OH groups of serines facilitate the formation of type [Al‐pep(H<jats:sub>‐1</jats:sub>)] complexes with the involvement of all carboxylategroups in the molecule. The relevance of intramolecular and intermolecular Al<jats:sup>3+</jats:sup> binding to the controversial biological role of aluminium is also discussed. © 1995 John Wiley & Sons, Inc.</jats:p>

収録刊行物

  • Biopolymers

    Biopolymers 36 (3), 381-389, 1995-09

    Wiley

被引用文献 (1)*注記

もっと見る

詳細情報 詳細情報について

問題の指摘

ページトップへ