TY - JOUR
T1 - Cordymin, an antifungal peptide from the medicinal fungus Cordyceps militaris
AU - Wong, Jack H.
AU - Ng, Tzi Bun
AU - Wang, Hexiang
AU - Sze, Stephen Cho Wing
AU - Zhang, Kalin Yanbo
AU - Li, Qi
AU - Lu, Xiaoxu
N1 - Acknowledgment:
The award of a direct grant from the Medicine Panel, CUHK Research Committee is gratefully acknowledged.
Publisher copyright:
© 2010 Elsevier GmbH. All rights reserved
PY - 2011/3/15
Y1 - 2011/3/15
N2 - Cordymin, an antifungal peptide with a molecular mass of 10,906 Da and an N-terminal amino acid sequence distinct from those of previously reported proteins, was purified from the medicinal mushroom Cordyceps militaris. The isolation protocol comprised ion exchange chromatography of the aqueous extract on SP-Sepharose and Mono S and gel filtration on Superdex 75 by a fast protein liquid chromatography system. Cordymin was adsorbed on both cation exchangers. The peptide inhibited mycelial growth in Bipolaris maydis, Mycosphaerella arachidicola, Rhizoctonia solani and Candida albicans with an IC50 of 50 μM, 10 μM, 80 μM, and 0.75 mM, respectively. However, there was no effect on Aspergillus fumigatus, Fusarium oxysporum and Valsa mali when tested up to 2 mM. The antifungal activity of the peptide was stable up to 100 °C and in the pH range 6–13, and unaffected by 10 mM Zn2+ and 10 mM Mg2+. Cordymin inhibited HIV-1 reverse transcriptase with an IC50 of 55 μM. Cordymin displayed antiproliferative activity toward breast cancer cells (MCF-7) but there was no effect on colon cancer cells (HT-29). There was no mitogenic activity toward mouse spleen cells and no nitric oxide inducing activity toward mouse macrophages when tested up to 1 mM.
AB - Cordymin, an antifungal peptide with a molecular mass of 10,906 Da and an N-terminal amino acid sequence distinct from those of previously reported proteins, was purified from the medicinal mushroom Cordyceps militaris. The isolation protocol comprised ion exchange chromatography of the aqueous extract on SP-Sepharose and Mono S and gel filtration on Superdex 75 by a fast protein liquid chromatography system. Cordymin was adsorbed on both cation exchangers. The peptide inhibited mycelial growth in Bipolaris maydis, Mycosphaerella arachidicola, Rhizoctonia solani and Candida albicans with an IC50 of 50 μM, 10 μM, 80 μM, and 0.75 mM, respectively. However, there was no effect on Aspergillus fumigatus, Fusarium oxysporum and Valsa mali when tested up to 2 mM. The antifungal activity of the peptide was stable up to 100 °C and in the pH range 6–13, and unaffected by 10 mM Zn2+ and 10 mM Mg2+. Cordymin inhibited HIV-1 reverse transcriptase with an IC50 of 55 μM. Cordymin displayed antiproliferative activity toward breast cancer cells (MCF-7) but there was no effect on colon cancer cells (HT-29). There was no mitogenic activity toward mouse spleen cells and no nitric oxide inducing activity toward mouse macrophages when tested up to 1 mM.
KW - Antifungal
KW - Isolation
KW - Cordyceps
UR - https://www.scopus.com/inward/record.uri?eid=2-s2.0-79952737572&doi=10.1016%2fj.phymed.2010.07.010&partnerID=40&md5=74c2722a6fdd74917a60c6a5a0abcc99
U2 - 10.1016/j.phymed.2010.07.010
DO - 10.1016/j.phymed.2010.07.010
M3 - Journal article
SN - 0944-7113
VL - 18
SP - 387
EP - 392
JO - Phytomedicine
JF - Phytomedicine
IS - 5
ER -