6WPB

NMR Structure of HSP1-NH2 antimicrobial peptide in presence of SDS-d25 micelles

Summary for 6WPB

• Entry DOI: 10.2210/pdb6wpb/pdb
• NMR Information: BMRB: 30744
• Descriptor: HSP1-NH2 (1 entity in total)
• Functional Keywords: antimicrobial peptide, antimicrobial protein
• Biological source: Boana punctata
• Total number of polymer chains: 1
• Total formula weight: 1311.59

Authors

Verly, R.M.,Gomes, I.P. (deposition date: 2020-04-27, release date: 2020-09-02, Last modification date: 2024-10-16)

Primary citation

Gomes, I.P.,Santos, T.L.,de Souza, A.N.,Nunes, L.O.,Cardoso, G.A.,Matos, C.O.,Costa, L.M.F.,Liao, L.M.,Resende, J.M.,Verly, R.M.
Membrane interactions of the anuran antimicrobial peptide HSP1-NH2: Different aspects of the association to anionic and zwitterionic biomimetic systems.
Biochim Biophys Acta Biomembr, 1863:183449-183449, 2020

PubMed Abstract: Studies have suggested that antimicrobial peptides act by different mechanisms, such as micellisation, self-assembly of nanostructures and pore formation on the membrane surface. This work presents an extensive investigation of the membrane interactions of the 14 amino-acid antimicrobial peptide hylaseptin P1-NH (HSP1-NH), derived from the tree-frog Hyla punctata, which has stronger antifungal than antibacterial potential. Biophysical and structural analyses were performed and the correlated results were used to describe in detail the interactions of HSP1-NH with zwitterionic and anionic detergent micelles and phospholipid vesicles. HSP1-NH presents similar well-defined helical conformations in both zwitterionic and anionic micelles, although NMR spectroscopy revealed important structural differences in the peptide N-terminus. H exchange experiments of HSP1-NH indicated the insertion of the most N-terminal residues (1-3) in the DPC-d micelles. A higher enthalpic contribution was verified for the interaction of the peptide with anionic vesicles in comparison with zwitterionic vesicles. The pore formation ability of HSP1-NH (examined by dye release assays) and its effect on the size and surface charge as well as on the lipid acyl chain ordering (evaluated by Fourier-transform infrared spectroscopy) of anionic phospholipid vesicles showed membrane disruption even at low peptide-to-phospholipid ratios, and the effect increases proportionately to the peptide concentration. On the other hand, these biophysical investigations showed that a critical peptide-to-phospholipid ratio around 0.6 is essential for promoting disruption of zwitterionic membranes. In conclusion, this study demonstrates that the binding process of the antimicrobial HSP1-NH peptide depends on the membrane composition and peptide concentration.

PubMed: 32828849
DOI: 10.1016/j.bbamem.2020.183449

Experimental method

SOLUTION NMR