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Membrane interaction and secondary structure of de novo designed arginine-and tryptophan peptides with dual function

Hanna Rydberg (Institutionen för kemi- och bioteknik, Fysikalisk kemi) ; Nils Carlsson (Institutionen för kemi- och bioteknik, Fysikalisk kemi) ; Bengt Nordén (Institutionen för kemi- och bioteknik, Fysikalisk kemi)
Biochemical and Biophysical Research Communications (0006-291X). Vol. 427 (2012), 2, p. 261-265.
[Artikel, refereegranskad vetenskaplig]

Cell-penetrating peptides and antimicrobial peptides are two classes of positively charged membrane active peptides with several properties in common. The challenge is to combine knowledge about the membrane interaction mechanisms and structural properties of the two classes to design peptides with membrane-specific actions, useful either as transporters of cargo or as antibacterial substances. Membrane active peptides are commonly rich in arginine and tryptophan. We have previously designed a series of arg/trp peptides and investigated how the position and number of tryptophans affect cellular uptake. Here we explore the antimicrobial properties and the interaction with lipid model membranes of these peptides, using minimal inhibitory concentrations assay (MIC), circular dichroism (CD) and linear dichroism (LD). The results show that the arg/trp peptides inhibit the growth of the two gram positive strains Staphylococcus aureus and Staphylococcus pyogenes, with some individual variations depending on the position of the tryptophans. No inhibition of the gram negative strains Proteus mirabilis or Pseudomonas aeruginosa was noticed. CD indicated that when bound to lipid vesicles one of the peptides forms an a-helical like structure, whereas the other five exhibited rather random coiled structures. LD indicated that all six peptides were somehow aligned parallel with the membrane surface. Our results do not reveal any obvious connection between membrane interaction and antimicrobial effect for the studied peptides. By contrast cell-penetrating properties can be coupled to both the secondary structure and the degree of order of the peptides.

Nyckelord: Cell-penetrating peptide, Arginine-rich peptide, Tryptophan, Antimicrobial peptide, Circular, cell-penetrating peptides, antimicrobial peptides, circular-dichroism, linear dichroism, lipid-membranes, rich peptides, melittin, orientation, mechanisms, bacteria



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Denna post skapades 2012-12-12.
CPL Pubid: 167577

 

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Institutioner (Chalmers)

Institutionen för kemi- och bioteknik, Fysikalisk kemi (2005-2014)

Ämnesområden

Energi
Livsvetenskaper
Materialvetenskap
Nanovetenskap och nanoteknik
Biokemi och molekylärbiologi

Chalmers infrastruktur