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A comparative CD and fluorescence study of a series of model calcium-binding peptides

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Goch G., Kozlowska H., Wojtowicz A., Bierzynski A.

Acta Biochimica Polonica

1999

tom 46

nr 3

Lanthanide-saturated peptides analogous to calcium-binding loops of EF-hand proteins can be used to stabilize the α-helical structure of peptide or protein segments attached to their C-termini. To study conformational properties of such loop-containing hybrids it is necessary to produce them in bacteria. In peptides obtained in this way the helix will be destabilized by the negatively charged C-terminal α-carboxyl groups. We propose to blocke them by the homoserine lactone. The results presented in this paper indicate that the presence of the lactone even at the C-terminus of the loop does not have any negative effect on the loop helix-nucleation ability. On the other hand, the presence of the α-NH+3 at the loop N-terminus leads to a drop of metal-binding constant and loss of the rigid structure of the α-helical segment of the loop. The α-amino group separated by one glycine residue from the loop N-terminus should also be avoided because it perturbs the conformation of the N-terminal part of the loop and may reduce the loop affinity to lanthanide ions.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Bierzynski A.

1 Goch G.

1 Kozlowska H.

1 Wojtowicz A.

1 1999

Wyniki wyszukiwania

A comparative CD and fluorescence study of a series of model calcium-binding peptides