Applications of Circular Dichroism for Structural Analysis of Gelatin and Antimicrobial Peptides

International Journal of Molecular Sciences

Ramamourthy Gopal¹  Jin Soon Park²  Chang Ho Seo³ 

[1] Research Center for Proteineous Materials, Chosun University, Gwangju 501-759, Korea; E-Mail:;Department of Biotechnology, Chosun University, Gwangju 501-759, Korea; E-Mail:;Department of Bioinformatics, Kongju National University, Kongju, South Korea; E-Mail:

关键词: circular dichroism;    antimicrobial peptides;    reduced glutathione;    gelatin;    sodium dodecyl sulfate;    Tween 80;    cell wall components;    lipopolysaccharide;   

DOI  :  10.3390/ijms13033229

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.