AI Chat Paper
Note: Please note that the following content is generated by AMiner AI. SciOpen does not take any responsibility related to this content.
{{lang === 'zh_CN' ? '文章概述' : 'Summary'}}
{{lang === 'en_US' ? '中' : 'Eng'}}
Chat more with AI
Powered by AMiner. Clicking this button will take you away from SciOpen.
Home Food Science of Animal Products Article
PDF (2.7 MB)
Cite
EndNote(RIS) BibTeX
Collect
Submit Manuscript AI Chat Paper
Show Outline
Outline
Show full outline
Hide outline
Outline
Show full outline
Hide outline
Review Article | Open Access

Role of food protein-derived peptides in the treatment of colon cancer

Xue Deng1, Jing Yang2, Huayi Suo1, Jiajia Song1( )
College of Food Science, Southwest University, Chongqing 400715, China
School of Food Science and Engineering, Chongqing Technology and Business University, Chongqing 400067, China
Show Author Information

Abstract

Colon cancer is one of the leading causes of cancer-related deaths and the second most common cancer in Western countries. Despite the availability of various treatment modalities, these therapies have not been fully successful due to their limited effectiveness and serious side effects. As a result, an increasing number of researchers are focusing on the search for natural active substances as potential agents for the treatment and prevention of colon cancer. Bioactive peptides derived from proteins play an important role in maintaining body functions. Several in vivo and in vitro studies have demonstrated that protein peptides can help prevent and mitigate colon cancer. This paper, therefore, explores the mitigating effects and mechanisms of action of protein peptides from different sources on colon cancer, as well as the factors influencing their anticancer effects. It provides a scientific basis for the prevention and treatment of colon cancer and for the development of new raw materials for foods with potential anticancer properties.

Keywords

proteinhydrolysatepeptidecolon cancer

References

[1]

N. Keum, E. H. Giovannucci, Global burden of colorectal cancer: emerging trends, risk factors and prevention strategies, Nat. Rev. Gastroenterol. Hepatologyl. 16 (2019) 713–732. https://doi.org/10.1038/s41575-019-0189-8.
Crossref Google Scholar
[2]

R. L. Siegel, A. N. Giaquinto, A. Jemal, Cancer statistics, 2024, CA: Cancer J. Clin. 74 (2024) 12–49. https://doi.org/10.3322/caac.21820.
Crossref Google Scholar
[3]

P. A. Newcomb, J. Baron, M. Cotterchio, et al., Colon cancer family registry: an international resource for studies of the genetic epidemiology of colon cancer, Cancer Epidemiol. Biomarker. Prev. 16 (2007) 2331–2343. https://doi.org/10.1158/1055-9965.EPI-07-0648.
Crossref Google Scholar
[4]

T. Sawicki, M. Ruszkowska, A. Danielewicz, et al., A review of colorectal cancer in terms of epidemiology, risk factors, development, symptoms and diagnosis, Cancers 13 (2021) 2025. https://doi.org/10.3390/cancers13092025.
Crossref Google Scholar
[5]

M. Ahmed, Colon cancer: a clinician’s perspective in 2019, Gastroenterol. Res. 13 (2020) 1–10. https://doi.org/10.14740/gr1239.
Crossref Google Scholar
[6]

M. L. Slattery, S. L. Edwards, K. M. Boucher, et al., Lifestyle and colon cancer: an assessment of factors associated with risk, Am. J. Epidemiol. 150 (1999) 869–877. https://doi.org/10.1093/oxfordjournals.aje.a010092.
Crossref Google Scholar
[7]

C. Cao, T. D. Yan, D. Black, et al., A systematic review and meta-analysis of cytoreductive surgery with perioperative intraperitoneal chemotherapy for peritoneal carcinomatosis of colorectal origin, Ann. Surg. Oncol. 16 (2009) 2152–2165. https://doi.org/10.1245/s10434-009-0487-4.
Crossref Google Scholar
[8]

L. Lemoine, P. Sugarbaker, K. van der Speeten, Pathophysiology of colorectal peritoneal carcinomatosis: role of the peritoneum, World J. Gastroenterol. 22 (2016) 7692. https://doi.org/10.3748/wjg.v22.i34.7692.
Crossref Google Scholar
[9]

P. H. Sugarbaker, Improving oncologic outcomes for colorectal cancer at high risk for local-regional recurrence with novel surgical techniques, Expert Rev. Gastroenterol. Hepatol. 10 (2016) 205–213. https://doi.org/10.1586/17474124.2016.1110019.
Crossref Google Scholar
[10]

D. Groza, S. Gehrig, P. Kudela, et al., Bacterial ghosts as adjuvant to oxaliplatin chemotherapy in colorectal carcinomatosis, Oncoimmunology 7 (2018) e1424676. https://doi.org/10.1080/2162402x.2018.1424676.
Crossref Google Scholar
[11]

T. Rustad, Utilisation of marine by-products, Electron. J. Environ. Agric. Food Chem. 2 (2003) 458–463.
Google Scholar
[12]

M. I. Shaik, N. M. Sarbon, A review on purification and characterization of anti-proliferative peptides derived from fish protein hydrolysate, Food Rev. Int. 38 (2022) 1389–1409. https://doi.org/10.1080/87559129.2020.1812634.
Crossref Google Scholar
[13]

A. Pihlanto-Leppälä, Bioactive peptides derived from bovine whey proteins: opioid and ace-inhibitory peptides, Trends Food Sci. Technol. 11 (2000) 347–356. https://doi.org/10.1016/S0924-2244(01)00003-6.
Crossref Google Scholar
[14]

M. Chalamaiah, W. L. Yu, J. P. Wu, Immunomodulatory and anticancer protein hydrolysates (peptides) from food proteins: a review, Food Chem. 245 (2018) 205–222. https://doi.org/10.1016/j.foodchem.2017.10.087.
Crossref Google Scholar
[15]

M. Chalamaiah, R. Hemalatha, T. Jyothirmayi, Fish protein hydrolysates: proximate composition, amino acid composition, antioxidant activities and applications: a review, Food Chem. 135 (2012) 3020–3038. https://doi.org/10.1016/j.foodchem.2012.06.100.
Crossref Google Scholar
[16]

S. Umayaparvathi, S. Meenakshi, V. Vimalraj, et al., Antioxidant activity and anticancer effect of bioactive peptide from enzymatic hydrolysate of oyster ( Saccostrea cucullata), Biomed. Prev. Nutr. 4 (2014) 343–353. https://doi.org/10.1016/j.bionut.2014.04.006.
Crossref Google Scholar
[17]

Z. Bhat, S. Kumar, H. F. Bhat, Bioactive peptides of animal origin: a review, J. Food Sci. Technol. 52 (2015) 5377–5392. https://doi.org/10.1007/s13197-015-1731-5.
Crossref Google Scholar
[18]

N. Halim, H. Yusof, N. Sarbon, Functional and bioactive properties of fish protein hydolysates and peptides: a comprehensive review, Trends Food Sci. Technol. 51 (2016) 24–33. https://doi.org/10.1016/j.jpgs.2016.02.007.
Crossref Google Scholar
[19]

M. González-Montoya, B. Hernández-Ledesma, J. M. Silván, et al., Peptides derived from in vitro gastrointestinal digestion of germinated soybean proteins inhibit human colon cancer cells proliferation and inflammation, Food Chem. 242 (2018) 75–82. https://doi.org/10.1016/j.foodchem.2017.09.035.
Crossref Google Scholar
[20]

X. J. Ji, J. Wang, A. J. Ma, et al., Effects of silkworm pupa protein on apoptosis and energy metabolism in human colon cancer DLD-1 cells, Food Sci. Hum. Well. 11 (2022) 1171–1176. https://doi.org/10.1016/j.fshw.2022.04.011.
Crossref Google Scholar
[21]

K. Hasani, P. Ariaii, M. Ahmadi, Antimicrobial, antioxidant and anti-cancer properties of protein hydrolysates from Indian mackerel ( Rastrelliger kanagurta) waste prepared using commercial enzyme, Int. J. Pept. Res. Ther. 28 (2022) 86. https://doi.org/10.1007/s10989-022-10396-z.
Crossref Google Scholar
[22]

A. Allaoui, S. Gascón, S. Benomar, et al., Protein hydrolysates from fenugreek ( Trigonella foenum graecum) as nutraceutical molecules in colon cancer treatment, Nutrients 11 (2019) 724. https://doi.org/10.3390/nu11040724.
Crossref Google Scholar
[23]

S. J. Rayaprolu, N. S. Hettiarachchy, P. Y. Chen, et al., Peptides derived from high oleic acid soybean meals inhibit colon, liver and lung cancer cell growth, Food Res. Int. 50 (2013) 282–288. https://doi.org/10.1016/j.foodres.2012.10.021.
Crossref Google Scholar
[24]

D. A. L. Vital, E. G. de Mejía, V. P. Dia, et al., Peptides in common bean fractions inhibit human colorectal cancer cells, Food Chem. 157 (2014) 347–355. https://doi.org/10.1016/j.foodchem.2014.02.050.
Crossref Google Scholar
[25]

V. P. Dia, E. G. de Mejia, Lunasin promotes apoptosis in human colon cancer cells by mitochondrial pathway activation and induction of nuclear clusterin expression, Cancer Lett. 295 (2010) 44–53. https://doi.org/10.1016/j.canlet.2010.02.010.
Crossref Google Scholar
[26]

R. Jahanbani, S. M. Ghaffari, M. Salami, et al., Antioxidant and anticancer activities of walnut ( Juglans regia L.) protein hydrolysates using different proteases, Plant Foods Hum. Nutr. 71 (2016) 402–409. https://doi.org/10.1007/s11130-016-0576-z.
Crossref Google Scholar
[27]

A. Akbarmehr, S. H. Peighambardoust, B. Ghanbarzadeh, et al., Physicochemical, antioxidant, antimicrobial, and in vitro cytotoxic activities of corn pollen protein hydrolysates obtained by different peptidases, Food Sci. Nutr. 11 (2023) 2403–2417. https://doi.org/10.1002/fsn3.3252.
Crossref Google Scholar
[28]
V. P. Dia, H. B. Krishnan, BG-4, a novel anticancer peptide from bitter gourd (Momordica charantia), promotes apoptosis in human colon cancer cells, Sci. Rep. 6 (2016) 33532. https://doi.org/10.1038/srep33532.
Crossref
[29]

V. Wattayagorn, M. Kongsema, S. Tadakittisarn, et al., Riceberry rice bran protein hydrolyzed fractions induced apoptosis, senescence and G1/S cell cycle arrest in human colon cancer cell lines, Appl. Sci. 12 (2022) 6917. https://doi.org/10.3390/app12146917.
Crossref Google Scholar
[30]
A. Kannan, N. Hettiarachchy, S. Narayan, Colon and breast anti-cancer effects of peptide hydrolysates derived from rice bran, Open Bioact. Compd. J. 2 (2009) 17–20. https://doi.org/10.2174/1874847300902010017.
Crossref
[31]

S. H. Shan, Z. W. Li, I. P. Newton, et al., A novel protein extracted from foxtail millet bran displays anti-carcinogenic effects in human colon cancer cells, Toxicol. Lett. 227 (2014) 129–138. https://doi.org/10.1016/j.toxlet.2014.03.008.
Crossref Google Scholar
[32]

M. Zhang, T. H. Mu, Contribution of different molecular weight fractions to anticancer effect of sweet potato protein hydrolysates by six proteases on HT-29 colon cancer cells, Int. J. Food Sci. Technol. 53 (2018) 525–532. https://doi.org/10.1111/ijfs.13625.
Crossref Google Scholar
[33]

A. Kannan, N. S. Hettiarachchy, J. O. Lay, et al., Human cancer cell proliferation inhibition by a pentapeptide isolated and characterized from rice bran, Peptides 31 (2010) 1629–1634. https://doi.org/10.1016/j.peptides.2010.05.018.
Crossref Google Scholar
[34]

X. Fan, H. M. Guo, C. Teng, et al., Anti-colon cancer activity of novel peptides isolated from in vitro digestion of quinoa protein in Caco-2 cells, Foods. 11 (2022) 194. https://doi.org/10.3390/foods11020194.
Crossref Google Scholar
[35]

J. Xie, Z. S. Hong, J. J. Dai, et al., Isolation and identification of anti-colorectal cancer peptides from walnut proteins and associated in silico analysis, J. Funct. Foods 112 (2024) 105952. https://doi.org/10.1016/j.jff.2023.105952.
Crossref Google Scholar
[36]

X. Fan, H. M. Guo, C. Teng, et al., Supplementation of quinoa peptides alleviates colorectal cancer and restores gut microbiota in AOM/DSS-treated mice, Food Chem. 408 (2023) 135196. https://doi.org/10.1016/j.foodchem.2022.135196.
Crossref Google Scholar
[37]

C. Gao, R. Sun, Y. R. Xie, et al., The soy-derived peptide Vglycin inhibits the growth of colon cancer cells in vitro and in vivo, Exp. Biol. Med. 242 (2017) 1034–1043. https://doi.org/10.1177/1535370217697383.
Crossref Google Scholar
[38]

D. A. Luna-Vital, E. González de Mejía, G. Loarca-Piña, Dietary peptides from Phaseolus vulgaris L. reduced AOM/DSS-induced colitis-associated colon carcinogenesis in Balb/c mice, Plant Foods Hum. Nutr. 72 (2017) 445–447. https://doi.org/10.1007/s11130-017-0633-2.
Crossref Google Scholar
[39]

F. Tonolo, A. Folda, V. Scalcon, et al., Nrf2-activating bioactive peptides exert anti-inflammatory activity through inhibition of the NF-κB pathway, Int. J. Mol. Sci. 23 (2022) 4382. https://doi.org/10.3390/ijms23084382.
Crossref Google Scholar
[40]
M. S. Sansi, D. Iram, S. Vij, et al., In vitro biosafety and bioactivity assessment of the goat milk protein derived hydrolysates peptides, J. Food Saf. 43 (2023) e13061. https://doi.org/10.1111/jfs.13061.
Crossref
[41]

R. L. Jiang, B. Lönnerdal, Bovine lactoferrin and lactoferricin exert antitumor activities on human colorectal cancer cells (HT-29) by activating various signaling pathways, Biochem. Cell Biol. 95 (2017) 99–109. https://doi.org/10.1139/bcb-2016-0094.
Crossref Google Scholar
[42]

J. H. Lee, S. H. Moon, H. S. Kim, et al., Antioxidant and anticancer effects of functional peptides from ovotransferrin hydrolysates, J. Sci. Food Agric. 97 (2017) 4857–4864. https://doi.org/10.1002/jsfa.8356.
Crossref Google Scholar
[43]
C. Murali, P. Mudgil, C.-Y. Gan, et al., Camel whey protein hydrolysates induced G2/M cellcycle arrest in human colorectal carcinoma, Sci. Rep. 11 (2021) 7062. https://doi.org/10.1038/s41598-021-86391-z.
Crossref
[44]

L. J. You, M. M. Zhao, R. H. Liu, et al., Antioxidant and antiproliferative activities of loach ( Misgurnus anguillicaudatus) peptides prepared by papain digestion, J. Agric. Food Chem. 59 (2011) 7948–7953. https://doi.org/10.1021/jf2016368.
Crossref Google Scholar
[45]

M. N. Yousr, A. A. Aloqbi, U. M. Omar, et al., Antiproliferative activity of egg yolk peptides in human colon cancer cells, Nutr. Cancer 69 (2017) 674–681. https://doi.org/10.1080/01635581.2017.1295087.
Crossref Google Scholar
[46]

B. N. P. Sah, T. Vasiljevic, S. McKechnie, et al., Antioxidant peptides isolated from synbiotic yoghurt exhibit antiproliferative activities against HT-29 colon cancer cells, Int. Dairy J. 63 (2016) 99–106. https://doi.org/10.1016/j.idairyj.2016.08.003.
Crossref Google Scholar
[47]

H. M. Habib, W. H. Ibrahim, R. Schneider-Stock, et al., Camel milk lactoferrin reduces the proliferation of colorectal cancer cells and exerts antioxidant and DNA damage inhibitory activities, Food Chem. 141 (2013) 148–152. https://doi.org/10.1016/j.foodchem.2013.03.039.
Crossref Google Scholar
[48]

C. Freiburghaus, C. Welinder, U. Tjörnstad, et al., Identification of ubiquitin in bovine milk and its growth inhibitory effects on human cancer cell lines, J. Dairy Sci. 93 (2010) 3442–3452. https://doi.org/10.3168/jds.2009-2878.
Crossref Google Scholar
[49]

S. E. El-Didamony, M. H. Kalaba, M. H. Sharaf, et al., Melittin alcalase-hydrolysate: a novel chemically characterized multifunctional bioagent; antibacterial, anti-biofilm and anticancer, Front. Microbiol. 15 (2024) 1419917. https://doi.org/10.3389/fmicb.2024.1419917.
Crossref Google Scholar
[50]

P. Maraming, S. Maijaroen, S. Klaynongsruang, et al., Antitumor ability of KT2 peptide derived from leukocyte peptide of crocodile against human HCT116 colon cancer xenografts, In Vivo 32 (2018) 1137–1144. https://doi.org/10.21873/invivo.11356.
Crossref Google Scholar
[51]
H. Tsuda, K. Sekine, J. Nakamura, et al., Inhibition of azoxymethane initiated colon tumor and aberrant crypt foci development by bovine lactoferrin administration in F344 rats, in: G. Spik, D. Legrand, J. Mazurier, et al. (Eds.), Advances in lactoferrin research. Advances in experimental medicine and biology, Springer, Boston, MA, 1998, pp. 273–284. https://doi.org/10.1007/978-1-4757-9068-9_34.
Crossref
[52]

R. Hakkak, S. Korourian, M. J. Ronis, et al., Dietary whey protein protects against azoxymethane-induced colon tumors in male rats, Cancer Epidemiol. Biomarker. Prev. 10 (2001) 555–558.
Google Scholar
[53]

T. Kozu, G. Iinuma, Y. Ohashi, et al., Effect of orally administered bovine lactoferrin on the growth of adenomatous colorectal polyps in a randomized, placebo-controlled clinical trial, Cancer Prev. Res. 2 (2009) 975–983. https://doi.org/10.1158/1940-6207.CAPR-08-0208.
Crossref Google Scholar
[54]

R. Suttisuwan, S. Phunpruch, T. Saisavoey, et al., Free radical scavenging properties and induction of apoptotic effects of FA fraction obtained after proteolysis of bioactive peptides from microalgae Synechococcus sp. VDW, Food Technol. Biotechnol. 57 (2019) 358–368. https://doi.org/10.17113/ftb.57.03.19.6028.
Crossref Google Scholar
[55]

Z. J. Wang, X. W. Zhang, Isolation and identification of anti-proliferative peptides from Spirulina platensis using three-step hydrolysis, J. Sci. Food Agric. 97 (2017) 918–922. https://doi.org/10.1002/jsfa.7815.
Crossref Google Scholar
[56]
M. Darvish, H. Jalili, S.-O. Ranaei-Siadat, et al., Potential cytotoxic effects of peptide fractions from Dunaliella salina protein hydrolyzed by gastric proteases, J. Aquat. Food Prod. Technol. 27 (2018) 165–175. https://doi.org/10.1080/10498850.2017.1414095.
Crossref
[57]

S. L. Minic, D. Stanic-Vucinic, J. Mihailovic, et al., Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin, a blue-colored biliprotein of microalga Spirulina, J. Proteomics 147 (2016) 132–139. https://doi.org/10.1016/j.jprot.2016.03.043.
Crossref Google Scholar
[58]

S. Umayaparvathi, M. Arumugam, S. Meenakshi, et al., Purification and characterization of antioxidant peptides from oyster ( Saccostrea cucullata) hydrolysate and the anticancer activity of hydrolysate on human colon cancer cell lines, Int. J. Pept. Res. Ther. 20 (2014) 231–243. https://doi.org/10.1007/s10989-013-9385-5.
Crossref Google Scholar
[59]

C. L. Li, S. R. Zhang, J. H. Zhu, et al., A novel peptide derived from Arca inflata induces apoptosis in colorectal cancer cells through mitochondria and the p38 MAPK pathway, Mar. Drugs 20 (2022) 110. https://doi.org/10.3390/md20020110.
Crossref Google Scholar
[60]

Z. Yaghoubzadeh, F. Peyravii Ghadikolaii, H. Kaboosi, et al., Antioxidant activity and anticancer effect of bioactive peptides from rainbow trout ( Oncorhynchus mykiss) skin hydrolysate, Int. J. Pept. Res. Ther. 26 (2020) 625–632. https://doi.org/10.1007/s10989-019-09869-5.
Crossref Google Scholar
[61]

R. Nurdiani, T. Vasiljevic, T. Yeager, et al., Bioactive peptides with radical scavenging and cancer cell cytotoxic activities derived from Flathead ( Platycephalus fuscus) by-products, Eur. Food Res. Technol. 243 (2017) 627–637. https://doi.org/10.1007/s00217-016-2776-z.
Crossref Google Scholar
[62]

A. Kannan, N. S. Hettiarachchy, M. Marshall, et al., Shrimp shell peptide hydrolysates inhibit human cancer cell proliferation, J. Sci. Food Agric. 91 (2011) 1920–1924. https://doi.org/10.1002/jsfa.4464.
Crossref Google Scholar
[63]

J. Chumchalová, J. Šmarda, Human tumor cells are selectively inhibited by colicins, Folia Microbiol. 48 (2003) 111–115. https://doi.org/10.1007/BF02931286.
Crossref Google Scholar
[64]

K. I. Villarante, F. B. Elegado, S. Iwatani, et al., Purification, characterization and in vitro cytotoxicity of the bacteriocin from Pediococcus acidilactici K2a2-3 against human colon adenocarcinoma (HT29) and human cervical carcinoma (HeLa) cells, World J. Microbiol. Biotechnol. 27 (2011) 975–980. https://doi.org/10.1007/s11274-010-0541-1.
Crossref Google Scholar
[65]

S. Maher, S. McClean, Investigation of the cytotoxicity of eukaryotic and prokaryotic antimicrobial peptides in intestinal epithelial cells in vitro, Biochem. Pharmacol. 71 (2006) 1289–1298. https://doi.org/10.1016/j.bcp.2006.01.012.
Crossref Google Scholar
[66]

Z. Norouzi, A. Salimi, R. Halabian, et al., Nisin, a potent bacteriocin and anti-bacterial peptide, attenuates expression of metastatic genes in colorectal cancer cell lines, Microb. Pathog. 123 (2018) 183–189. https://doi.org/10.1016/j.micpath.2018.07.006.
Crossref Google Scholar
[67]

M. A. Varas, C. Muñoz-Montecinos, V. Kallens, et al., Exploiting zebrafish xenografts for testing the in vivo antitumorigenic activity of microcin E492 against human colorectal cancer cells, Front. Microbiol. 11 (2020) 405. https://doi.org/10.3389/fmicb.2020.00405.
Crossref Google Scholar
[68]

C. Freiburghaus, B. Janicke, H. Lindmark-Månsson, et al., Lactoferricin treatment decreases the rate of cell proliferation of a human colon cancer cell line, J. Dairy Sci. 92 (2009) 2477–2484. https://doi.org/10.3168/jds.2008-1851.
Crossref Google Scholar
[69]

V. P. Dia, E. G. De Mejia, Lunasin induces apoptosis and modifies the expression of genes associated with extracellular matrix and cell adhesion in human metastatic colon cancer cells, Mol. Nutr. Food Res. 55 (2011) 623–634. https://doi.org/10.1002/mnfr.201000419.
Crossref Google Scholar
[70]

L. Y. Su, Y. X. Shi, M. R. Yan, et al., Anticancer bioactive peptides suppress human colorectal tumor cell growth and induce apoptosis via modulating the PARP-p53-Mcl-1 signaling pathway, Acta Pharmacol. Sin. 36 (2015) 1514–1519. https://doi.org/10.1038/aps.2015.80.
Crossref Google Scholar
[71]

D. A. Luna-Vital, K. Liang, E. G. De Mejía, et al., Dietary peptides from the non-digestible fraction of Phaseolus vulgaris L. decrease angiotensin II-dependent proliferation in HCT116 human colorectal cancer cells through the blockade of the renin-angiotensin system, Food Funct. 7 (2016) 2409–2419. https://doi.org/10.1039/C6FO00093B.
Crossref Google Scholar
[72]

X. Y. Li, J. F. Sun, S. Q. Hu, The renin-angiotensin system blockers as adjunctive therapy for cancer: a meta-analysis of survival outcome, Eur. Rev. Med. Pharmacol. Sci. 21 (2017) 1375–1383.
Google Scholar
[73]

R. van der Knaap, C. Siemes, J. W. W. Coebergh, et al., Renin-angiotensin system inhibitors, angiotensin I-converting enzyme gene insertion/deletion polymorphism, and cancer: the Rotterdam study, Cancer 112 (2008) 748–757. https://doi.org/10.1002/cncr.23215.
Crossref Google Scholar
[74]

H. W. Li, Y. F. Qi, C. Y. Li, et al., Angiotensin type 2 receptor-mediated apoptosis of human prostate cancer cells, Mol. Cancer Ther. 8 (2009) 3255–3265. https://doi.org/10.1158/1535-7163.MCT-09-0237.
Crossref Google Scholar
[75]

E. Nuti, L. Rosalia, D. Cuffaro, et al., Bifunctional inhibitors as a new tool to reduce cancer cell invasion by impairing MMP-9 homodimerization, ACS Med. Chem. Lett. 8 (2017) 293–298. https://doi.org/10.1021/acsmedchemlett.6b00446.
Crossref Google Scholar
[76]

A. Lima, J. Mota, S. Monteiro, et al., Legume seeds and colorectal cancer revisited: protease inhibitors reduce MMP-9 activity and colon cancer cell migration, Food Chem. 197 (2016) 30–38. https://doi.org/10.1016/j.foodchem.2015.10.063.
Crossref Google Scholar
[77]

E. B. M. Daliri, B. H. Lee, D. H. Oh, Current trends and perspectives of bioactive peptides, Crit. Rev. Food Sci. Nutr. 58 (2018) 2273–2284. https://doi.org/10.1080/10408398.2017.1319795.
Crossref Google Scholar
[78]

L. A. Tejano, J. P. Peralta, E. E. S. Yap, et al., Prediction of bioactive peptides from Chlorella sorokiniana proteins using proteomic techniques in combination with bioinformatics analyses, Int. J. Mol. Sci. 20 (2019) 1786. https://doi.org/10.3390/ijms20071786.
Crossref Google Scholar
[79]

M. A. Ali, M. M. Kamal, M. H. Rahman, et al., Functional dairy products as a source of bioactive peptides and probiotics: current trends and future prospectives, J. Food Sci. Technol. 59 (2022) 1263–1279. https://doi.org/10.1007/s13197-021-05091-8.
Crossref Google Scholar
[80]

D. Bhandari, S. Rafiq, Y. Gat, et al., A review on bioactive peptides: physiological functions, bioavailability and safety, Int. J. Pept. Res. Ther. 26 (2020) 139–150. https://doi.org/10.1007/s10989-019-09823-5.
Crossref Google Scholar
[81]

C. C. Udenigwe, V. Fogliano, Food matrix interaction and bioavailability of bioactive peptides: two faces of the same coin?, J. Funct. Foods 35 (2017) 9–12. https://doi.org/10.1016/j.jff.2017.05.029.
Crossref Google Scholar
[82]

N. Ishak, N. Sarbon, A review of protein hydrolysates and bioactive peptides deriving from wastes generated by fish processing, Food Bioprocess Technol. 11 (2018) 2–16. https://doi.org/10.1007/s11947-017-1940-1.
Crossref Google Scholar
[83]

W. Chiangjong, S. Chutipongtanate, S. Hongeng, Anticancer peptide: physicochemical property, functional aspect and trend in clinical application, Int. J. Oncol. 57 (2020) 678–696. https://doi.org/10.3892/ijo.2020.5099.
Crossref Google Scholar
[84]

Y. X. Dai, X. G. Cai, W. Shi, et al., Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane, Amino Acids 49 (2017) 1601–1610. https://doi.org/10.1007/s00726-017-2453-y.
Crossref Google Scholar
[85]

H. Korhonen, A. Pihlanto-Leppäla, P. Rantamäki, et al., Impact of processing on bioactive proteins and peptides, Trends Food Sci. Technol. 9 (1998) 307–319. https://doi.org/10.1016/S0924-2244(98)00054-5.
Crossref Google Scholar
[86]

L. Liu, S. S. Li, J. X. Zheng, et al., Safety considerations on food protein-derived bioactive peptides, Trends Food Sci. Technol. 96 (2020) 199–207. https://doi.org/10.1016/j.jpgs.2019.12.022.
Crossref Google Scholar
[87]

L. M. Beltrán-Barrientos, H. S. García, M. J. Torres-Llanez, et al., Safety of milk-derived bioactive peptides, Int. J. Dairy Technol. 70 (2017) 16–22. https://doi.org/10.1111/1471-0307.12338.
Crossref Google Scholar
[88]

R. J. FitzGerald, B. A. Murray, D. J. Walsh, Hypotensive peptides from milk proteins, J. Nutr. 134 (2004) 980S–988S. https://doi.org/10.1093/jn/134.4.980S.
Crossref Google Scholar
[89]

X. H. Sun, C. Acquah, R. E. Aluko, et al., Considering food matrix and gastrointestinal effects in enhancing bioactive peptide absorption and bioavailability, J. Funct. Foods 64 (2020) 103680. https://doi.org/10.1016/j.jff.2019.103680.
Crossref Google Scholar
[90]

L. Ramezanzade, S. F. Hosseini, M. Nikkhah, Biopolymer-coated nanoliposomes as carriers of rainbow trout skin-derived antioxidant peptides, Food Chem. 234 (2017) 220–229. https://doi.org/10.1016/j.foodchem.2017.04.177.
Crossref Google Scholar
Food Science of Animal Products
Volume 2 Issue 4,
December 2024
Article number: 9240087
DOI: 10.26599/FSAP.2024.9240087
Cite this article:
Deng X, Yang J, Suo H, et al. Role of food protein-derived peptides in the treatment of colon cancer. Food Science of Animal Products, 2024, 2(4): 9240087. https://doi.org/10.26599/FSAP.2024.9240087

270

Views

56

Downloads

0

Crossref

Altmetrics
Received: 20 August 2024
Revised: 29 September 2024
Accepted: 08 October 2024
Published: 08 January 2025
© Beijing Academy of Food Sciences 2024.

Food Science of Animal Products published by Tsinghua University Press. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
Return