2N0O

NMR Solution Structure and Model Membrane Interaction Studies of the Peptide Hylin a1 from the Arboreal South American Frog Hypsiboas albopunctatus

Summary for 2N0O

• Entry DOI: 10.2210/pdb2n0o/pdb
• NMR Information: BMRB: 25529
• Descriptor: Hylin-a1 (1 entity in total)
• Functional Keywords: antimicrobial protein
• Biological source: Hypsiboas albopunctatus (Spotted tree frog)
• Cellular location: Secreted : P85982
• Total number of polymer chains: 1
• Total formula weight: 1865.37

Authors

Alves, E.S.F.,Oliveira, A.L. (deposition date: 2015-03-11, release date: 2015-06-24, Last modification date: 2024-10-09)

Primary citation

Alves, E.S.,Junior, E.C.,Cilli, E.M.,Castro, M.S.,Fontes, W.,de Magalhaes, M.T.,Liao, L.M.,de Oliveira, A.L.
Micelle Bound Structure and Model Membrane Interaction Studies of the Peptide Hylin a1 from the Arboreal South American Frog Hypsiboas albopunctatus.
Protein Pept.Lett., 22:719-726, 2015

PubMed Abstract: Antimicrobial peptides (AMPs) appear as a promising therapeutic candidate against multiresistant pathogens, because they are able to kill microorganisms and have low toxicity of resistance cells. Hylin a1 (Hy-a1, IFGAILPLALGALKNLIK-NH2) is a peptide extracted from the skin secretion of the frog Hypsiboas albopunctatus, which displays antimicrobial and hemolytic activities. We report here structural studies of Hy-a1 using different techniques such as fluorescence, CD and NMR. Our data showed that Hy-a1 acquires a well defined amphipathic α-helix when interacting with a membrane-like environment. Furthermore, Hy-a1 presented different affinity when compared to membranes of zwitterionic or anionic lipid composition. Finally, we proposed a molecular interaction model of this peptide with micelles.

PubMed: 26059694

Experimental method

SOLUTION NMR