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The effect of methylmercury(II) binding on the conformation of poly(L-glutamic acid) and poly(L-lysine): A raman spectroscopic study

✍ Scribed by S. Alex; H. A. Tajmir-Riahi; R. Savoie

Publisher: Wiley (John Wiley & Sons)
Year: 1987
Tongue: English
Weight: 631 KB
Volume: 26
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.360260816

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✦ Synopsis

The binding of the methylmercury cation CH3Hg+ by poly(L-glutamic acid) (PGA) and by poly(i-lysine) (PLL) has been investigated by b a n spectroscopy. Coordination on the side-chain COO-and NH; groups of these polypeptides gave characteristic ligand-Hg stretching modes at ca. 505 and 450 cm-', respectively. Precipitation generally occurred upon formation of the complexes and changes of conformation were common. The solid complex obtained from PGA at pH 4.6 was found to have a mostly disordered conformation, which differed from the respective a-helical and /?-sheet structures of the &olved and precipitated uncomplexed polypeptide in the same conditions. An a-helical structure was generally adopted by the complex formed with PLL, even in pH and temperature conditions where the free polypeptide normally exists in another conformation. The addition of a stronger complexing agent, glutathione, to the PLL/CH3Hg+ complex caused a migration of the bound cations and a restoration of the polypeptide to its original state.

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