RT Journal Article
T1 Roles of amphipathicity and hydrophobicity in the micelle-driven structural switch of a 14-mer peptide core from a Choline-binding repeat
A1 Zamora Carreras, Héctor
A1 Maestro García-Donas, María Beatriz
A1 Strandberg, Eric
A1 Ulrich, Anne
A1 Sanz, Jesús
A1 Jiménez, María Ángeles
AB Choline-binding repeats (CBRs) are ubiquitous sequences with a β-hairpin core that are found in the surface proteins of several microorganisms such as S. pneumoniae (pneumococcus). Previous studies on a 14-mer CBR sequence derived from the pneumoccal LytA autolysin (LytA239–252 peptide) have demonstrated a switch behaviour for this peptide, so that it acquires a stable, native-like β-hairpin conformation in aqueous solution but is reversibly transformed into an amphipathic α-helix in the presence of detergent micelles. With the aim of understanding the factors responsible for this unusual β-hairpin to α-helix transition, and to specifically assess the role of peptide hydrophobicity and helical amphipathicity in the process, we designed a series of LytA239–252 variants affecting these two parameters and studied their interaction with dodecylphosphocholine (DPC) micelles by solution NMR, circular dichroism and fluorescence spectroscopies. Our results indicate that stabilising cross-strand interactions become essential for β-hairpin stability in the absence of optimal turn sequences. Moreover, both amphipathicity and hydrophobicity display comparable importance for helix stabilisation of CBR-derived peptides in micelles, indicating that these sequences represent a novel class of micelle/membrane-interacting peptides.
PB Wiley
SN 0947-6539
YR 2018
FD 2018
LK https://hdl.handle.net/20.500.14352/96984
UL https://hdl.handle.net/20.500.14352/96984
LA eng
NO Zamora‐Carreras, Héctor, et al. «Roles of Amphipathicity and Hydrophobicity in the Micelle‐Driven Structural Switch of a 14‐mer Peptide Core from a Choline‐Binding Repeat». Chemistry – A European Journal, vol. 24, n.o 22, abril de 2018, pp. 5825-39. https://doi.org/10.1002/chem.201704802.
NO This work was supported by the Spanish MINECO grants (co-financed by European FEDER funds): CTQ2017-84371-P, CTQ2014-52633-P, BIO2016-79323-R and BIO2013-47684-R; and by the German Helmholtz Gemeinschaft. H. Zamora-Carreras was a recipient of a FPI scholarship (BES-2012-057717), and his stay at KIT, Germany was financed by the Spanish MINECO short stay grant EEBB-I-14-08805.
NO Helmholtz Association of German Research Centres
NO European Commission
NO Ministerio de Economía y Competitividad (España)
DS Docta Complutense
RD 6 abr 2025