Human semen contains a large number of macromolecules， including proteins/enzymes and carbohydrates， regulating and protecting sperm cells. Proteomic analysis of human seminal fluid led to the discovery of semen amyloids derived from short peptide fragments of the proteins prostatic acid phosphatase (PAP) and semenogelin (SG) which are known to play a crucial role in enhancing HIV infection. However， the relevance of their existence in human semen and role in maintaining sperm behavior remains unclear. Distinct physiological， biochemical， and biophysical attributes might cause these amyloids to influence sperm behavior positively or negatively， affecting fertilization or other reproductive processes. We assessed the direct effect of amyloids derived from a PAP fragment， on sperm motility and viability， which are crucial parameters for assessment of sperm quality in semen. Co-incubation of human sperm with PAP amyloids at normal physiological concentrations formed in buffer led to significant reduction in sperm viability， though approximately?a 10× higher concentration was needed to show a similar effect with amyloid formed in seminal fluid. Both forms of PAP amyloid also had a significant impact on sperm motility at physiological levels， in agreement with a previous report. Our study suggests that PAP amyloids can directly influence sperm motility and viability in a concentration-dependent manner. We hypothesise that the direct toxic effect of PAP amyloid is normally mitigated by other seminal fluid ingredients， but that in pathological conditions， where PAP concentrations are elevated and it plays a role in determining sperm health and viability， with relevance for male fertility as well as sterility.