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Proceedings of the Estonian Academy of Sciences

ISSN 1736-7530 (electronic)   ISSN 1736-6046 (print)
Formerly: Proceedings of the Estonian Academy of Sciences, series Physics & Mathematics and  Chemistry
Published since 1952

Proceedings of the Estonian Academy of Sciences

ISSN 1736-7530 (electronic)   ISSN 1736-6046 (print)
Formerly: Proceedings of the Estonian Academy of Sciences, series Physics & Mathematics and  Chemistry
Published since 1952
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The effect of solvent composition on complex formation of S100B protein with peptides; pp. 67–72

(Full article in PDF format) doi: 10.3176/proc.2009.1.12


Authors

Heiki Vija, Tõnu Kesvatera

Abstract

Complex formation of a vertebrate calcium sensor protein S100B with peptides  TRTKIDWNKILS (A) and SHLKSKKGQSTSRHKKLMWKTE (B) was studied. In contrast with previous reports, the affinity of these peptides for S100B was found to be similar. Added DTT, CaCl2, NaCl, and change in pH differentially reduce the affinity of the two peptides up to two orders of magnitude in the studied range. The effect of added salt is more pronounced for binding peptide B with a higher positive net charge. We conclude that it is necessary to have carefully controlled media conditions in affinity measurements of S100B protein with its targets. This is important in search for efficient S100B blockers of medical interest.

Keywords

bioorganic chemistry, S100B, protein, calcium sensor, peptide, charges, solvent.

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