P. Maloň,1 L. Bednárová,1 M. Kubáňová1, M. Urbanová2 and V. Baumruk3



1Institute of Organic Chemistry and Biochemistry, 166 10 Prague 6,
2Institute of Chemical Technology, 166 28 Prague 6
3Faculty of Mathematics and Physics, Charles University, 121 16 Prague 2

Disulfide group is an important structural constituent of peptides and proteins. It is a part of definition of protein primary structure, although it can be created /broken much easier than the general peptide chain forming linkage – the amide. Despite its evident importance for the peptide /protein structure the relation of its stereochemistry and spectroscopic properties is still not known at full detail.

We present here a comparison of our calculations on simple model disulfides [1] with experimental data obtained by spectroscopic investigation (especially chiroptical) of several rigid and semi-rigid model compounds. These include disulfide-bridged cyclodextrins [2] and neurohypophyseal hormone analogs [3]. We have attempted electronic spectroscopy and vibrational spectroscopy including their chiroptical variants – circular dichroism (ECD, VCD) and Raman optical activity (ROA).

1.      L. Bednárová, P. Bouř and P. Maloň, Chirality, accepted 2009.

2.      P. Maloň, L. Bednárová, M. Straka, L. Krejčí, L. Kumprecht, T. Kraus, M. Kubáňová, V. Baumruk, Chirality, accepted 2010.

3.      P. Maloň, L. Bednárová, H. Dlouhá, M. Flegel, J. Hlaváček, V. Setnička, M. Urbanová, S. Hynie, V. Klenerová, M. Kubáňová, V. Baumruk, Coll.Czech.Chem.Commun., submitted 2010.



This work was supported by Grant Agency of the Czech Republic (no. 203/07/1335 and P205/10/1276).