Antifungal　peptides　with　a　molecular　mass　of　9　kappa　Da　and　an　N-terminal　sequence　demonstrating　remarkable　similarity　to　those　of　nonspecific　lipid　transfer　proteins　(nsLTPs)　were　isolated　from　seeds　of　the　vegetable　Brassica　campestris　and　the　mung　bean.　The　purified　peptides　exerted　an　inhibitory　action　on　mycelial　growth　in　various　fungal　species.　The　antifungal　activity　of　Brassica　and　mung　bean　nsLTPs　were　thermostable,　pH-stable,　and　stable　after　treatment　with　pepsin　and　trypsin.　In　contrast,　the　antifungal　activity　of　mung　bean　chitinase　was　much　less　stable　to　changes　in　pH　and　temperature.　Brassica　LTP　inhibited　proliferation　of　hepatoma　Hep　G2　cells　and　breast　cancer　MCF　7　cells　with　an　IC50　of　5.8　and　1.6　mu　Mu,　respectively,　and　the　activity　of　HIV-1　reverse　transcriptase　with　an　IC50　of　4　mu　Mu.　However,　mung　bean　LTP　and　chitinase　were　devoid　of　antiproliferative　and　HIV-1　reverse　transcriptase　inhibitory　activities.　In　contrast　to　the　mung　bean　LTP,　which　exhibited　antibacterial　activity,　Brassica　LTP　was　inactive.　All　three　antifungal　peptides　lacked　mitogenic　activity　toward　splenocytes.　These　results　indicate　that　the　two　LTPs　have　more　desirable　activities　than　the　chitinase　and　that　there　is　a　dissociation　between　the　antifungal　and　other　activities　of　these　antifungal　proteins.　Copyright　(C)　2007　European　Peptide　Society　and　John　Wiley　&　Sons,　Ltd.