Editing Trypsin (section)

==Trypsin inhibitor==
{{main|Trypsin inhibitor}}
To prevent the action of active trypsin in the pancreas, which can be highly damaging, inhibitors such as [[BPTI]] and [[SPINK1]] in the pancreas and [[Alpha 1-antitrypsin|α1-antitrypsin]] in the serum are present as part of the defense against its inappropriate activation. Any trypsin prematurely formed from the inactive trypsinogen is then bound by the inhibitor. The protein-protein interaction between trypsin and its inhibitors is one of the tightest bound, and trypsin is bound by some of its pancreatic inhibitors nearly irreversibly.<ref>{{cite book | vauthors = Voet D, Voet JG | title = Biochemistry | pages = [https://archive.org/details/biochemistry00voet_0/page/396 396–400] | edition = 2nd | year = 1995 | publisher = John Wiley & Sons | isbn = 978-0-471-58651-7 | url = https://archive.org/details/biochemistry00voet_0/page/396 }}</ref>  In contrast with nearly all known protein assemblies, some complexes of trypsin bound by its inhibitors do not readily dissociate after treatment with 8M urea.<ref>{{cite journal | vauthors = Levilliers N, Péron M, Arrio B, Pudles J | title = On the mechanism of action of proteolytic inhibitors. IV. Effect of 8 M urea on the stability of trypsin in trypsin-inhibitor complexes | journal = Archives of Biochemistry and Biophysics | volume = 140 | issue = 2 | pages = 474–83 | date = October 1970 | pmid = 5528741 | doi = 10.1016/0003-9861(70)90091-3 }}</ref>

Trypsin inhibitors can serve as tools when addressing metabolic and obesity disorders. Metabolic disorders, obesity, and being overweight are known to increase non-communicable chronic disease prevalence.<ref name="Cristina_Oliveira_de_Lima_2019">{{cite journal | vauthors = Cristina Oliveira de Lima V, Piuvezam G, Leal Lima Maciel B, Heloneida de Araújo Morais A | title = Trypsin inhibitors: promising candidate satietogenic proteins as complementary treatment for obesity and metabolic disorders? | journal = Journal of Enzyme Inhibition and Medicinal Chemistry | volume = 34 | issue = 1 | pages = 405–419 | date = December 2019 | pmid = 30734596 | pmc = 6327991 | doi = 10.1080/14756366.2018.1542387 }}</ref> It is of public health policy interest to explore various ways to mitigate this occurrence including use of trypsin inhibitors. These inhibitors have capabilities of reducing colon, breast, skin, and prostate cancer by way of radioprotective and anticarcinogenic activity. Trypsin inhibitors can act as regulatory mechanisms to control release of neutrophil proteases and avoid significant tissue damage.<ref name="Cristina_Oliveira_de_Lima_2019" /> In regards to cardiovascular conditions associated with unproductive serine protease activity, trypsin inhibitors can block their activity in platelet aggregation, fibrinolysis, coagulation, and blood coagulation.

The multifunctionality of trypsin inhibitors includes being potential protease inhibitors for AMP activity.<ref name="de Souza Nascimento_2022">{{cite journal | vauthors = de Souza Nascimento AM, de Oliveira Segundo VH, Felipe Camelo Aguiar AJ, Piuvezam G, Souza Passos T, Florentino da Silva Chaves Damasceno KS, de Araújo Morais AH | title = Antibacterial action mechanisms and mode of trypsin inhibitors: a systematic review | journal = Journal of Enzyme Inhibition and Medicinal Chemistry | volume = 37 | issue = 1 | pages = 749–759 | date = December 2022 | pmid = 35168466 | pmc = 8856033 | doi = 10.1080/14756366.2022.2039918 }}</ref> While the antibacterial action mechanisms of trypsin inhibitors are unclear, studies have aimed to study their mechanisms as potential applications in bacterial infection treatments.<ref name="de Souza Nascimento_2022" /> Research and scanning microscopy showed antibacterial effects on bacterial membranes from ''[[Staphylococcus aureus]]''.<ref name="de Souza Nascimento_2022" /> Trypsin inhibitors from amphibian skin showed bacterial death promotion that affected the cell wall and membrane of ''Staphylococcus aureus''.<ref name="de Souza Nascimento_2022" /> Studies also analyzed antibacterial actions in trypsin inhibitor peptides, proteins, and ''[[Escherichia coli|E. coli]]''. The results showed sufficient bacterial growth prevention. However, trypsin inhibitors have to meet certain criteria to be utilized in foods and medical treatments.<ref name="de Souza Nascimento_2022" />