%0 Journal Article
%A Maestro García-Donas, María Beatriz
%A Santiveri, C. M.
%A Jimenez, M. A.
%A Sanz, J. M.
%T Structural autonomy of a beta-hairpin peptide derived from the pneumococcal choline-binding protein LytA
%D 2010
%@ 1741-0126
%U https://hdl.handle.net/20.500.14352/93162
%X The cell wall of Streptococcus pneumoniae and several other micro-organisms is decorated with a number of the so-called choline-binding proteins (CBPs) that recognise the choline residues in the bacterial surface by means of highly conserved, concatenated 20-aa sequences termed choline-binding repeats (CBRs), that are composed of a loop and a β-hairpin structure. In this work, we have investigated the ability to fold in aqueous solution of a 14-aa peptide (LytA197–210[wt]) and a single derivative of it, LytA197–210[ND], corresponding to one of the six β-hairpins of the LytA pneumococcal amidase. Intrinsic fluorescence and circular dichroism spectroscopical measurements showed that both peptides spontaneously acquire a non-random conformation which is also able to bind the natural ligand choline. Furthermore, nuclear magnetic resonance techniques allowed the calculation of the structure of the LytA197–210[ND] peptide, which displayed a β-hairpin conformation highly similar to that found within the full-length C-LytA module. These results provide a structural basis for the modular organisation of CBPs and suggest the use of CBRs as new templates for the design of stable β-hairpins.
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