%0 Journal Article
%T Isolation and Purification of a Novel Deca-Antifungal Peptide from Potato (Solanum tuberosum L. cv. Jopung) Against Candida albicans
%A Jong-Kook Lee
%A Ramamourthy Gopal
%A Chang Ho Seo
%A Hyeonsook Cheong
%A Yoonkyung Park
%J International Journal of Molecular Sciences
%D 2012
%I MDPI AG
%R 10.3390/ijms13044021
%X In a previous study, an antifungal protein, AFP-J, was purified from tubers of the potato ( Solanum tuberosum cv. L Jopung) and by gel filtration and HPLC. In this study, the functional peptide was characterized by partial acid digestion using HCl and HPLC. We obtained three peaks from the AFP-J, the first and third peaks were not active in the tested fungal strain. However, the second peak, which was named Potide-J, was active (MIC; 6.25 ¦Ìg/mL) against Candida albicans. The amino acid sequences were analyzed by automated Edman degradation, and the amino acid sequence of Potide-J was determined to be Ala-Val-Cys-Glu-Asn-Asp-Leu-Asn-Cys-Cys. Mass spectrometry showed that its molecular mass was 1083.1 Da. Finally, we confirmed that a disulfide bond was present between Cys 3 and Cys 9 or Cys 10. Using this structure, Potide-J was synthesized via solid-phase methods. In these experiments, only the linear sequence was shown to display strong activity against Candida albicans. These results suggest that Potide-J may be an excellent candidate compound for the development of commercially applicable antibiotic agents.
%K AFP-J
%K partial acid digestion
%K Potide-J
%K antibiotic agent
%U http://www.mdpi.com/1422-0067/13/4/4021