How Insertion of a Single Tryptophan in the N-Terminus of a Cecropin A-Melittin Hybrid Peptide Changes Its Antimicrobial and Biophysical Profile

Autor:	Paula Gameiro, Carla F. Sousa, Paula Gomes, Cátia Teixeira, Lucinda J. Bessa, Ana Rita Ferreira
Přispěvatelé:	HIRI, Helmholtz-Institut für RNA-basierte Infektionsforschung, Josef-Shneider Strasse 2, 97080 Würzburg, Germany.
Rok vydání:	2021
Předmět:	cation-π interactions membrane-targeting activity 0301 basic medicine antibiotic resistance 030106 microbiology Lysine large unilamellar vesicles Filtration and Separation Peptide lcsh:Chemical technology Article Melittin 03 medical and health sciences chemistry.chemical_compound cecropin-melittin peptides medicine Chemical Engineering (miscellaneous) lcsh:TP1-1185 tryptophan lcsh:Chemical engineering chemistry.chemical_classification Chemistry Process Chemistry and Technology Vesicle Tryptophan lcsh:TP155-156 030104 developmental biology Membrane Mechanism of action Biophysics CAMP medicine.symptom Antibacterial activity
Zdroj:	Membranes Switzerland Membranes, Vol 11, Iss 48, p 48 (2021) Volume 11 Issue 1
ISSN:	2077-0375
DOI:	10.3390/membranes11010048
Popis:	In the era of antibiotic resistance, there is an urgent need for efficient antibiotic therapies to fight bacterial infections. Cationic antimicrobial peptides (CAMP) are promising lead compounds given their membrane-targeted mechanism of action, and high affinity towards the anionic composition of bacterial membranes. We present a new CAMP, W-BP100, derived from the highly active BP100, holding an additional tryptophan at the N-terminus. W-BP100 showed a broader antibacterial activity, demonstrating a potent activity against Gram-positive strains. Revealing a high partition constant towards anionic over zwitterionic large unilamellar vesicles and inducing membrane saturation at a high peptide/lipid ratio, W-BP100 has a preferential location for hydrophobic environments. Contrary to BP100, almost no aggregation of anionic vesicles is observed around saturation conditions and at higher concentrations no aggregation is observed. With these results, it is possible to state that with the incorporation of a single tryptophan to the N-terminus, a highly active peptide was obtained due to the &pi &ndash electron system of tryptophan, resulting in negatively charged clouds, that participate in cation&ndash &pi interactions with lysine residues. Furthermore, we propose that W-BP100 action can be achieved by electrostatic interactions followed by peptide translocation.
Databáze:	OpenAIRE
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