Conformational Study of the Antimicrobial Peptide Melectin by Circular Dichroism Methods

Authors

  • S. Kykal Department of Analytical Chemistry, Faculty of Chemical Engineering, Institute of Chemical Technology, Prague
  • V. Čeřovský Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Prague
  • V. Setnička Department of Analytical Chemistry, Faculty of Chemical Engineering, Institute of Chemical Technology, Prague,

Keywords:

antimicrobial peptides, conformation, circular dichroism

Abstract

Antimicrobial peptides are considered as promising supplements to or substitutes for conventional antibiotics due to their different mechanisms of action. Biological activities of antimicrobial peptides are influenced by their conformations. The solution conformations of 18 amino acid residues peptide melectin (MEP) and its synthetic analogues including C-terminal and N-terminal fragments were studied using electronic and vibrational circular dichroism spectroscopies.

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Published

2013-03-15

How to Cite

Kykal, S., Čeřovský, V., & Setnička, V. (2013). Conformational Study of the Antimicrobial Peptide Melectin by Circular Dichroism Methods. Chemické Listy, 107(3), 250–254. Retrieved from http://w.chemicke-listy.cz/ojs3/index.php/chemicke-listy/article/view/751

Issue

Vol. 107 No. 3 (2013)

Section

Articles