Scorpion venom is a rich source of biologically active peptides that act in different systems, such as nervous and cardiovascular. Facilities in using micro-scale analytical techniques, such as mass spectrometry and proteomics, have led to a novel approach to prospect bioactive molecules in animal venoms. This is based on a structural-guided prospection and can lead to discover of novel functional molecules that have not yet been visualized by conventional bioassays and pharmacological-guided methods. By this prospection approach, we were able to find a new structural family of peptides in the venom of the Brazilian yellow scorpion Tityus serrulatus, named TsHpTP (Tityus serrulatus HypoTensive Peptides). Structurally, these are random-coiled linear peptides, ranging from 2500 to 3000 Da and have a typical bradykinin-potentiating peptide (BPP) amino acid signature. TsHpT-I (2722.43 Da), a member of these peptide family, was able to potentiate the hypotensive effects of bradykinin (BK) in normotensive rats. To optimize the pharmacokinetics and the stability of TsHpT-I, few synthetic analogs (ranging from 953.51 to 482.38 Da) were constructed using TsHpT-I as template. These analogs held the bradykinin-potentiating effect observed on the native peptide. Also, a relevant hypotensive effect, which is independent on BK, was observed in all of these analogs, indicating that they are themselves hypotensive agents. We used two hypertensive rats strains (SHR and TGR) to study this hypotensive effect and it has been shown that these analogs induces a strong and long-lasting hypotensive effect. To evaluate the hypotensive action of these analogs, we examined the vasorelaxation effect of aortic rings derived from male Wistar rats. They were able to induce about 20% of vasorelaxation (10^-7 M). The 482.38 Da analog was orally administrated in SHR rats and was able to reduce the blood pressure, indicating that this analog is stable and can be absorbed in the gastrointestinal tract. The mode of action of these analogs is yet to be solved, but it seems that Angiotensin Converting Enzyme, a well known BPP target, is not the primary target. Instead, preliminary data using CHO cells with transfected B₂ receptor, carried out in confocal microscopy, has shown that these analogs are able to potentiate the NO release induced by BK, although the molecular mechanism of this potentiation is not clear yet.