Higher plants, microorganisms, and marine organisms are rich sources of cyclic  peptides, and recently, much attention has been devoted to these macromolecules due to their variety of essential biological functions. As part of our continuing investigation of new biologically active natural products, we have focused our attention on the isolation of cyclic peptides from the Euphorbiaceous plants. The fractionation and isolation methodologies development, structure elucidation, and biological activity of peptide from Angiospermae is a pioneering study in Brazil, and in this study we reported the isolation, characterization, and biological activity of two peptides 1 and 2 isolated from Jatropha multifida L., collected in São Paulo state. The latex from this plant was partitioned with ethyl acetate, fractioned on Sephadex G15, eluted in solid phase extraction (SEPACK-C18) and purified by HPLC, and the presence of peptide was detected by Cl₂/o-tolidine reagent. The characterization of these compounds was performed by amino acid analysis after acid hydrolysis (6N HCl at 110 ^oC for 24 h in a seled tube) and posterior analysis of the molecular weight, and amino acid sequence by mass analysis using a triple quadrupole mass spectrometer (Quattro-LC, Micromass). The molecular weight of peptide 1 was 1049,0 g/mol, and peptide 2 was 869,0 g/mol, respectively. The sequence obtained by mass spectrometry was GVWTVWGTIA to 1 and  ISAAWGIGI to peptide 2, both connected by a head-tail bond. In order to confirm the amino acids sequence of 1, it was cleaved by Chymotrypsin and the fragments produced were separated by HPLC and sequenced separately by Edman procedure. The biological effects of  1 and 2 were examined against phytopathogenic fungi Cladosporium cladosporioides and C. sphaerospermum, and  acetylcholinesterase (AChE) TLC bioautography assays. [FAPESP, CNPq, FINEP]