Abstract
Circular dichroism (CD) is a useful technique for monitoring changes in the conformation of antimicrobial peptides or gelatin. In this study, interactions between cationic peptides and gelatin were observed without affecting the triple helical content of the gelatin, which was more strongly affected by anionic surfactant. The peptides did not adopt a secondary structure in the presence of aqueous solution or Tween 80, but a peptide secondary structure formed upon the addition of sodium dodecyl sulfate (SDS). The peptides bound to the phosphate group of lipopolysaccharide (LPS) and displayed an alpha-helical conformation while (KW)4 adopted a folded conformation. Further, the peptides did not specifically interact with the fungal cell wall components of mannan or laminarin. Tryptophan blue shift assay indicated that these peptides interacted with SDS, LPS, and gelatin but not with Tween 80, mannan, or laminarin. The peptides also displayed antibacterial activity against P. aeruginosa without cytotoxicity against HaCaT cells at MIC, except for HPA3NT3-analog peptide. In this study, we used a CD spectroscopic method to demonstrate the feasibility of peptide characterization in numerous environments. The CD method can thus be used as a screening method of gelatin-peptide interactions for use in wound healing applications.
Highlights
Circular dichroism (CD) spectroscopy is the most widespread technique used for estimating the secondary structures of proteins and polypeptides in solution [1]
Gelatin is a protein produced by acid and alkaline processing of collagen and is characterized by a three-chain structure in which individual helical chains are stranded in a superhelix about a common molecular axis [12,13,14]
Based on CD, we investigated whether or not Tween 80 causes changes in peptide conformation
Summary
Circular dichroism (CD) spectroscopy is the most widespread technique used for estimating the secondary structures of proteins and polypeptides in solution [1] This technique can be used to distinguish between unordered (random coil) and ordered (alpha-helix or beta-sheet) structures [2,3]. Most linear cationic antimicrobial peptides (AMPs) are in an unordered state in aqueous solution. As these molecules are amphipathic, they can adopt folded conformations in both hydrophobic and hydrophilic environments [4]. We synthesized (KW) peptide based on previous data showing that (KW) has antimicrobial activity [8]. The structures and organization of the peptides in aqueous solution, SDS, Tween 80, lipopolysaccharide (LPS), mannan, or laminarin were determined using CD spectroscopy. The antibacterial and cytotoxicity activities of the peptides were determined
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