Oxytocin
Nasally administered oxytocin has been reported to reduce fear, possibly by inhibiting the amygdala (which is thought to be responsible for fear responses). Indeed, studies in rodents have shown oxytocin can efficiently inhibit fear responses by activating an inhibitory circuit within the amygdala. Some researchers have argued oxytocin has a general enhancing effect on all social emotions, since intranasal administration of oxytocin also increases envy and "Schadenfreude". Individuals who receive an intranasal dose of oxytocin identify facial expressions of disgust more quickly than individuals who do not receive oxytocin. Facial expressions of disgust are evolutionarily linked to the idea of contagion. Thus, oxytocin increases the salience of cues that imply contamination, which leads to a faster response because these cues are especially relevant for survival. In another study, after administration of oxytocin, individuals displayed an enhanced ability to recognize expressions of fear compared to the individuals who received the placebo. Oxytocin modulates fear responses by enhancing the maintenance of social memories. Rats that are genetically modified to have a surplus of oxytocin receptors display a greater fear response to a previously conditioned stressor. Oxytocin enhances the aversive social memory, leading the rat to display a greater fear response when the aversive stimulus is encountered again.
Oxotoxin
Oxotoxins, or oxytoxins, are a group of neurotoxins present in the venom of lynx spiders belonging to the genus "Oxyopes", hence the name "oxytoxin". They are disulfide-rich peptides. Only two types are so far reported from two different species, the larger oxytoxin 1 (OxyTx1) from "Oxyopes kitabensis", and the smaller oxytoxin 2 (OxyTx2) from "Oxyopes lineatus". OxyTx1, the first known oxytoxin, was discovered in 2002. It was found to enhance the lethal efficacy of the spider venom by acting together with oxyopinins. It is composed of 69 amino acid residue, which are cross-linked by five disulfide bridges. It is a large peptide having a molecular mass of 8059.2 Da; but shows the size of 9,109.4 Da due to the presence of disulfide bridges. It is a potent insecticide, but non-toxic to mice up to 1 μg/20-g mouse. It acts synergistically with oxyopinins of the same venom to increase the insecticidal effect.