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Journal articles on the topic 'Anticancer peptides'

Author: Grafiati

Published: 4 June 2021

Last updated: 2 February 2022

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1

Ng, Chu Xin, and Sau Har Lee. "The Potential Use of Anticancer Peptides (ACPs) in the Treatment of Hepatocellular Carcinoma." Current Cancer Drug Targets 20, no. 3 (2020): 187–96. http://dx.doi.org/10.2174/1568009619666191111141032.

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Peptides have acquired increasing interest as promising therapeutics, particularly as anticancer alternatives during recent years. They have been reported to demonstrate incredible anticancer potentials due to their low manufacturing cost, ease of synthesis and great specificity and selectivity. Hepatocellular carcinoma (HCC) is among the leading cause of cancer death globally, and the effectiveness of current liver treatment has turned out to be a critical issue in treating the disease efficiently. Hence, new interventions are being explored for the treatment of hepatocellular carcinoma. Anticancer peptides (ACPs) were first identified as part of the innate immune system of living organisms, demonstrating promising activity against infectious diseases. Differentiated beyond the traditional effort on endogenous human peptides, the discovery of peptide drugs has evolved to rely more on isolation from other natural sources or through the medicinal chemistry approach. Up to the present time, the pharmaceutical industry intends to conduct more clinical trials for the development of peptides as alternative therapy since peptides possess numerous advantages such as high selectivity and efficacy against cancers over normal tissues, as well as a broad spectrum of anticancer activity. In this review, we present an overview of the literature concerning peptide’s physicochemical properties and describe the contemporary status of several anticancer peptides currently engaged in clinical trials for the treatment of hepatocellular carcinoma.

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2

Gabernet, G., A. T. Müller, J. A. Hiss, and G. Schneider. "Membranolytic anticancer peptides." MedChemComm 7, no. 12 (2016): 2232–45. http://dx.doi.org/10.1039/c6md00376a.

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3

Arias, Mauricio, Ashley L. Hilchie, Evan F. Haney, et al. "Anticancer activities of bovine and human lactoferricin-derived peptides." Biochemistry and Cell Biology 95, no. 1 (2017): 91–98. http://dx.doi.org/10.1139/bcb-2016-0175.

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Lactoferrin (LF) is a mammalian host defense glycoprotein with diverse biological activities. Peptides derived from the cationic region of LF possess cytotoxic activity against cancer cells in vitro and in vivo. Bovine lactoferricin (LFcinB), a peptide derived from bovine LF (bLF), exhibits broad-spectrum anticancer activity, while a similar peptide derived from human LF (hLF) is not as active. In this work, several peptides derived from the N-terminal regions of bLF and hLF were studied for their anticancer activities against leukemia and breast-cancer cells, as well as normal peripheral blood mononuclear cells. The cyclized LFcinB-CLICK peptide, which possesses a stable triazole linkage, showed improved anticancer activity, while short peptides hLF11 and bLF10 were not cytotoxic to cancer cells. Interestingly, hLF11 can act as a cell-penetrating peptide; when combined with the antimicrobial core sequence of LFcinB (RRWQWR) through either a Pro or Gly–Gly linker, toxicity to Jurkat cells increased. Together, our work extends the library of LF-derived peptides tested for anticancer activity, and identified new chimeric peptides with high cytotoxicity towards cancerous cells. Additionally, these results support the notion that short cell-penetrating peptides and antimicrobial peptides can be combined to create new adducts with increased potency.

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4

Juretić, Davor, Anja Golemac, Denise E. Strand, et al. "The Spectrum of Design Solutions for Improving the Activity-Selectivity Product of Peptide Antibiotics against Multidrug-Resistant Bacteria and Prostate Cancer PC-3 Cells." Molecules 25, no. 15 (2020): 3526. http://dx.doi.org/10.3390/molecules25153526.

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The link between the antimicrobial and anticancer activity of peptides has long been studied, and the number of peptides identified with both activities has recently increased considerably. In this work, we hypothesized that designed peptides with a wide spectrum of selective antimicrobial activity will also have anticancer activity, and tested this hypothesis with newly designed peptides. The spectrum of peptides, used as partial or full design templates, ranged from cell-penetrating peptides and putative bacteriocin to those from the simplest animals (placozoans) and the Chordata phylum (anurans). We applied custom computational tools to predict amino acid substitutions, conferring the increased product of bacteriostatic activity and selectivity. Experiments confirmed that better overall performance was achieved with respect to that of initial templates. Nine of our synthesized helical peptides had excellent bactericidal activity against both standard and multidrug-resistant bacteria. These peptides were then compared to a known anticancer peptide polybia-MP1, for their ability to kill prostate cancer cells and dermal primary fibroblasts. The therapeutic index was higher for seven of our peptides, and anticancer activity stronger for all of them. In conclusion, the peptides that we designed for selective antimicrobial activity also have promising potential for anticancer applications.

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Liscano, Yamil, Jose Oñate-Garzón, and Jean Paul Delgado. "Peptides with Dual Antimicrobial–Anticancer Activity: Strategies to Overcome Peptide Limitations and Rational Design of Anticancer Peptides." Molecules 25, no. 18 (2020): 4245. http://dx.doi.org/10.3390/molecules25184245.

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Peptides are naturally produced by all organisms and exhibit a wide range of physiological, immunomodulatory, and wound healing functions. Furthermore, they can provide with protection against microorganisms and tumor cells. Their multifaceted performance, high selectivity, and reduced toxicity have positioned them as effective therapeutic agents, representing a positive economic impact for pharmaceutical companies. Currently, efforts have been made to invest in the development of new peptides with antimicrobial and anticancer properties, but the poor stability of these molecules in physiological environments has triggered a bottleneck. Therefore, some tools, such as nanotechnology and in silico approaches can be applied as alternatives to try to overcome these obstacles. In silico studies provide a priori knowledge that can lead to the development of new anticancer peptides with enhanced biological activity and improved stability. This review focuses on the current status of research in peptides with dual antimicrobial–anticancer activity, including advances in computational biology using in silico analyses as a powerful tool for the study and rational design of these types of peptides.

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6

Aaghaz, Shams, Vivek Gohel, and Ahmed Kamal. "Peptides as Potential Anticancer Agents." Current Topics in Medicinal Chemistry 19, no. 17 (2019): 1491–511. http://dx.doi.org/10.2174/1568026619666190125161517.

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Cancer consists of heterogeneous multiple cell subpopulation which at a later stage develop resistant phenotypes, which include resistance to pro-apoptotic stimuli and/or cytotoxic resistance to anticancer compounds. The property of cancerous cells to affect almost any part of the body categorizes cancer to many anatomic and molecular subtypes, each requiring a particular therapeutic intervention. As several modalities are hindered in a variety of cancers and as the cancer cells accrue varied types of oncogenic mutations during their progression the most likely benefit will be obtained by a combination of therapeutic agents that might address the diverse hallmarks of cancer. Natural compounds are the backbone of cancer therapeutics owing to their property of affecting the DNA impairment and restoration mechanisms and also the gene expression modulated via several epigenetic molecular mechanisms. Bioactive peptides isolated from flora and fauna have transformed the arena of antitumour therapy and prompt progress in preclinical studies is promising. The difficulties in creating ACP rest in improving its delivery to the tumour site and it also must maintain a low toxicity profile. The substantial production costs, low selectivity and proteolytic stability of some ACP are some of the factors hindering the progress of peptide drug development. Recently, several publications have tried to edify the field with the idea of using peptides as adjuvants with established drugs for antineoplastic use. This review focuses on peptides from natural sources that precisely target tumour cells and subsequently serve as anticancer agents that are less toxic to normal tissues.

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7

Sun, Zhi-Gang, Zhi-Na Li, Bao-Chan Yang, and Liang-Hui Zhao. "Design and Synthesis of Novel Anticancer Peptide Nanoparticles." Journal of Drug Delivery and Therapeutics 10, no. 4 (2020): 102–7. http://dx.doi.org/10.22270/jddt.v10i4.4156.

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Cancer has now become a common disease affecting human health. Existing cancer treatment drugs can no longer meet the growing needs of cancer patients, and the emergence of anticancer drug resistance has exacerbated this phenomenon. By designing and synthesizing new anticancer peptide nanoparticles and studying their anticancer effects, new strategies for cancer treatment may be obtained. Novel anticancer peptides are synthesized by adding basic amino acids and solid-phase synthesis technology, and their structural information is determined by mass spectrometry. Nanoparticles of anticancer peptide were synthesized by nano-self-assembly technology. Two novel anticancer peptides exhibited anticancer activity, one of which was assembled into nanoparticles. The theoretical isoelectric points of the modified SZG3 and SZG5 are all greater than physiological pH, and will be positively charged under physiological conditions. The estimated half-life of SZG3 and SZG5 is significantly extended (30h), which is beneficial to increase the efficacy and reduce toxic and side effects. SZG3 and SZG5 have a good inhibitory effect on tumor cells and have low toxicity to normal cells. Keywords: anticancer peptide, study, design, cancer, nanoparticles

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8

Torres, Marcelo D. T., Gislaine P. Andrade, Roseli H. Sato, et al. "Natural and redesigned wasp venom peptides with selective antitumoral activity." Beilstein Journal of Organic Chemistry 14 (July 6, 2018): 1693–703. http://dx.doi.org/10.3762/bjoc.14.144.

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About 1 in 8 U.S. women (≈12%) will develop invasive breast cancer over the course of their lifetime. Surgery, chemotherapy, radiotherapy, and hormone manipulation constitute the major treatment options for breast cancer. Here, we show that both a natural antimicrobial peptide (AMP) derived from wasp venom (decoralin, Dec-NH2), and its synthetic variants generated via peptide design, display potent activity against cancer cells. We tested the derivatives at increasing doses and observed anticancer activity at concentrations as low as 12.5 μmol L−1 for the selective targeting of MCF-7 breast cancer cells. Flow cytometry assays further revealed that treatment with wild-type (WT) peptide Dec-NH2 led to necrosis of MCF-7 cells. Additional atomic force microscopy (AFM) measurements indicated that the roughness of cancer cell membranes increased significantly when treated with lead peptides compared to controls. Biophysical features such as helicity, hydrophobicity, and net positive charge were identified to play an important role in the anticancer activity of the peptides. Indeed, abrupt changes in peptide hydrophobicity and conformational propensity led to peptide inactivation, whereas increasing the net positive charge of peptides enhanced their activity. We present peptide templates with selective activity towards breast cancer cells that leave normal cells unaffected. These templates represent excellent scaffolds for the design of selective anticancer peptide therapeutics.

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Hilchie, Ashley L., Erin E. Gill, Melanie R. Power Coombs, Reza Falsafi, Robert E. W. Hancock, and David W. Hoskin. "MDA-MB-231 Breast Cancer Cells Resistant to Pleurocidin-Family Lytic Peptides Are Chemosensitive and Exhibit Reduced Tumor-Forming Capacity." Biomolecules 10, no. 9 (2020): 1220. http://dx.doi.org/10.3390/biom10091220.

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Direct-acting anticancer (DAA) peptides are cytolytic peptides that show promise as novel anticancer agents. DAA peptides bind to anionic molecules that are abundant on cancer cells relative to normal healthy cells, which results in preferential killing of cancer cells. Due to the mechanism by which DAA peptides kill cancer cells, it was thought that resistance would be difficult to achieve. Here, we describe the generation and characterization of two MDA-MB-231 breast cancer cell-line variants with reduced susceptibility to pleurocidin-family and mastoparan DAA peptides. Peptide resistance correlated with deficiencies in peptide binding to cell-surface structures, suggesting that resistance was due to altered composition of the cell membrane. Peptide-resistant MDA-MB-231 cells were phenotypically distinct yet remained susceptible to chemotherapy. Surprisingly, neither of the peptide-resistant breast cancer cell lines was able to establish tumors in immune-deficient mice. Histological analysis and RNA sequencing suggested that tumorigenicity was impacted by alternations in angiogenesis and extracellular matrix composition in the peptide-resistant MDA-MB-231 variants. Collectively, these data further support the therapeutic potential of DAA peptides as adjunctive treatments for cancer.

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10

Soon, Tsuey Ning, Adeline Yoke Yin Chia, Wei Hsum Yap, and Yin-Quan Tang. "Anticancer Mechanisms of Bioactive Peptides." Protein & Peptide Letters 27, no. 9 (2020): 823–30. http://dx.doi.org/10.2174/0929866527666200409102747.

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: Despite technological advancement, there is no 100% effective treatment against metastatic cancer. Increasing resistance of cancer cells towards chemotherapeutic drugs along with detrimental side effects remained a concern. Thus, the urgency in developing new anticancer agents has been raised. Anticancer peptides have been proven to display potent activity against a wide variety of cancer cells. Several mode of actions describing their cytostatic and cytotoxic effect on cancer cells have been proposed which involves cell surface binding leading to membranolysis or internalization to reach their intracellular target. Understanding the mechanism of action of these anticancer peptides is important in achieving full therapeutic success. In the present article, we discuss the anticancer action of peptides accompanied by the mechanisms underpinning their toxicity to cancer cells.

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11

Lin, Yen-Chu, Yi Fan Lim, Erica Russo, et al. "Multidimensional Design of Anticancer Peptides." Angewandte Chemie International Edition 54, no. 35 (2015): 10370–74. http://dx.doi.org/10.1002/anie.201504018.

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12

Gross, Stephanie, and Jörg Andrä. "Anticancer peptide NK-2 targets cell surface sulphated glycans rather than sialic acids." Biological Chemistry 393, no. 8 (2012): 817–27. http://dx.doi.org/10.1515/hsz-2012-0136.

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Abstract Some antimicrobial peptides have emerged as potential anticancer agents. In contrast to chemotherapeutics, they act primarily by physical disruption of the cancer cell membrane. Selective targeting of these cationic peptides still remains elusive. We focus on the interaction of α-helical peptides NK-2, cathelicidin LL32, and melittin with PC-3 prostate cancer cells, and we provide strong evidence that, amongst the anionic glycans covering the cell surface, sulphated carbohydrates rather than sialic acids are the preferred interaction sites of the peptides. To test the significance of cell surface carbohydrates, a glycan microarray screen with fluorescently labelled peptides has been performed. Amongst 465 mammalian glycan structures on the chip, more than 20 different sulphated glycans were detected as the preferred binding partners of the peptide NK-2. The amount of peptide bound to sialic acid containing oligosaccharides was close to background level. These findings were consistent with microcalorimetric experiments revealing high and low binding enthalpies of peptides to sulphated carbohydrates and to sialic acid, respectively. Enzymatic desialylation of PC-3 cells did not affect peptide-mediated changes in cell metabolism, cell membrane permeabilisation, killing rate, and kinetics. Finally, the cytotoxicity of all peptides could be drastically impaired through the competitive inhibition by chondroitin sulphate, but not by sialic acid and sialylated fetuin.

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13

Garizo, Ana Rita, Lígia F. Coelho, Sandra Pinto, et al. "The Azurin-Derived Peptide CT-p19LC Exhibits Membrane-Active Properties and Induces Cancer Cell Death." Biomedicines 9, no. 9 (2021): 1194. http://dx.doi.org/10.3390/biomedicines9091194.

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Peptides have been thoroughly studied as new therapeutic strategies for cancer treatment. In this work, we explored in vitro the anticancer potential of three novel peptides derived from the C-terminal of azurin, an anticancer bacterial protein produced by Pseudomonas aeruginosa. CT-p26, CT-p19 and CT-p19LC peptides were previously obtained through an in silico peptide design optimization process, CT-p19LC being the most promising as it presented higher hydrophobicity and solubility, positive total charge and, most importantly, greater propensity for anticancer activity. Therefore, in this study, through proliferation and apoptosis assays, CT-p19LC was tested in four cancer cell lines—A549, MCF-7, HeLa and HT-29—and in two non-cancer cell lines—16HBE14o- and MCF10A. Its membrane-targeting activity was further evaluated with zeta potential measurements and membrane order was assessed with the Laurdan probe. The results obtained demonstrated that CT-p19LC decreases cell viability through induction of cell death and binds to the plasma membrane of cancer cells, but not to non-cancer cells, making them less rigid. Overall, this study reveals that CT-p19LC is an auspicious selective anticancer peptide able to react with cancer cell membranes and cause effective action.

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14

Feng, Pengmian, and Zhenyi Wang. "Recent Advances in Computational Methods for Identifying Anticancer Peptides." Current Drug Targets 20, no. 5 (2019): 481–87. http://dx.doi.org/10.2174/1389450119666180801121548.

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Anticancer peptide (ACP) is a kind of small peptides that can kill cancer cells without damaging normal cells. In recent years, ACP has been pre-clinically used for cancer treatment. Therefore, accurate identification of ACPs will promote their clinical applications. In contrast to labor-intensive experimental techniques, a series of computational methods have been proposed for identifying ACPs. In this review, we briefly summarized the current progress in computational identification of ACPs. The challenges and future perspectives in developing reliable methods for identification of ACPs were also discussed. We anticipate that this review could provide novel insights into future researches on anticancer peptides.

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15

Qin, Yuan, Zuo D. Qin, Jing Chen, et al. "From Antimicrobial to Anticancer Peptides: The Transformation of Peptides." Recent Patents on Anti-Cancer Drug Discovery 14, no. 1 (2019): 70–84. http://dx.doi.org/10.2174/1574892814666190119165157.

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Background: Antimicrobial peptides play an important role in the innate immune system. Possessing broad-spectrum antibacterial activity, antimicrobial peptides can quickly treat and kill various targets, including gram-negative bacteria, gram-positive bacteria, fungi, and tumor cells.Objective:An overview of the state of play with regard to the research trend of antimicrobial peptides in recent years and the situation of targeting tumor cells, and to make statistical analysis of the patents related to anticancer peptides published in recent years, is important both from toxicological and medical tumor therapy point of view.Methods:Based on the Science Citation Index Expanded version, the Derwent Innovation Index and Innography as data sources, the relevant literature and patents concerning antimicrobial peptides and anticancer peptides were analyzed through the Thomson Data Analyzer. Results of toxicologic and pharmacologic studies that brought to the development of patents for methods to novel tumor drugs were analyzed and sub-divided according to the specific synthesis of anticancer peptides.Results:The literature and patent search data show that the research and development of global antimicrobial peptides and anticancer peptides has been in an incremental mode. Growing patent evidence indicate that bioinformatics technology is a valuable strategy to modify, synthesize or recombine existing antimicrobial peptides to obtain tumor drugs with high activity, low toxicity and multiple targets.Conclusion:These findings may have important clinical implications for cancer treatment, especially in patients with conditions that are not currently treatable by other drugs, or that are resistant to existing cancer drugs.

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Shahidi, Fereidoon, and Ying Zhong. "Bioactive Peptides." Journal of AOAC INTERNATIONAL 91, no. 4 (2008): 914–31. http://dx.doi.org/10.1093/jaoac/91.4.914.

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Abstract Peptides with biological activities, released during gastrointestinal digestion or food processing, play an important role in metabolic regulation and modulation, suggesting their potential use as nutraceuticals and functional food ingredients for health promotion and disease risk reduction. Many studies have reported that peptides from various food sources possess bioactivities, including antihypertensive, antioxidant, anticancer, antimicrobial, and opioid activities as well as immunomodulatory and cholesterol-lowering effects. More studies are being performed exploring the sources, bioavailabilities, and possible physiological/functional properties and the mechanisms of action of bioactive peptides. Technological approaches in terms of peptide preparation, purification, and characterization have also been investigated.

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Vernen, Felicitas, Peta J. Harvey, Susana A. Dias, et al. "Characterization of Tachyplesin Peptides and Their Cyclized Analogues to Improve Antimicrobial and Anticancer Properties." International Journal of Molecular Sciences 20, no. 17 (2019): 4184. http://dx.doi.org/10.3390/ijms20174184.

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Tachyplesin I, II and III are host defense peptides from horseshoe crab species with antimicrobial and anticancer activities. They have an amphipathic β-hairpin structure, are highly positively-charged and differ by only one or two amino acid residues. In this study, we compared the structure and activity of the three tachyplesin peptides alongside their backbone cyclized analogues. We assessed the peptide structures using nuclear magnetic resonance (NMR) spectroscopy, then compared the activity against bacteria (both in the planktonic and biofilm forms) and a panel of cancerous cells. The importance of peptide-lipid interactions was examined using surface plasmon resonance and fluorescence spectroscopy methodologies. Our studies showed that tachyplesin peptides and their cyclic analogues were most potent against Gram-negative bacteria and melanoma cell lines, and showed a preference for binding to negatively-charged lipid membranes. Backbone cyclization did not improve potency, but improved peptide stability in human serum and reduced toxicity toward human red blood cells. Peptide-lipid binding affinity, orientation within the membrane, and ability to disrupt lipid bilayers differed between the cyclized peptide and the parent counterpart. We show that tachyplesin peptides and cyclized analogues have similarly potent antimicrobial and anticancer properties, but that backbone cyclization improves their stability and therapeutic potential.

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Feng, Jue-Ping, Ru Zhu, Fagang Jiang, et al. "Melittin-encapsulating peptide hydrogels for enhanced delivery of impermeable anticancer peptides." Biomaterials Science 8, no. 16 (2020): 4559–69. http://dx.doi.org/10.1039/c9bm02080b.

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Rubin, Samuel J. S., and Nir Qvit. "Engineering “Antimicrobial Peptides” and Other Peptides to Modulate Protein-Protein Interactions in Cancer." Current Topics in Medicinal Chemistry 20, no. 32 (2020): 2970–83. http://dx.doi.org/10.2174/1568026620666201021141401.

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Antimicrobial peptides (AMPs) are a class of peptides found across a wide array of organisms that play key roles in host defense. AMPs induce selective death in target cells and orchestrate specific or nonspecific immune responses. Many AMPs exhibit native anticancer activity in addition to antibacterial activity, and others have been engineered as antineoplastic agents. We discuss the use of AMPs in the detection and treatment of cancer as well as mechanisms of AMP-induced cell death. We present key examples of cathelicidins and transferrins, which are major AMP families. Further, we discuss the critical roles of protein-protein interactions (PPIs) in cancer and how AMPs are well-suited to target PPIs based on their unique drug-like properties not exhibited by small molecules or antibodies. While peptides, including AMPs, can have limited stability and bioavailability, these issues can be overcome by peptide backbone modification or cyclization (e.g., stapling) and by the use of delivery systems such as cellpenetrating peptides (CPPs), respectively. We discuss approaches for optimizing drug properties of peptide and peptidomimetic leads (modified peptides), providing examples of promising techniques that may be applied to AMPs. These molecules represent an exciting resource as anticancer agents with unique therapeutic advantages that can target challenging mechanisms involving PPIs. Indeed, AMPs are suitable drug leads for further development of cancer therapeutics, and many studies to this end are underway.

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Dąbrowska, Krystyna, Zuzanna Kaźmierczak, Joanna Majewska, et al. "Bacteriophages displaying anticancer peptides in combined antibacterial and anticancer treatment." Future Microbiology 9, no. 7 (2014): 861–69. http://dx.doi.org/10.2217/fmb.14.50.

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Feng, Jue-Ping, Ru Zhu, Fagang Jiang, et al. "Correction: Melittin-encapsulating peptide hydrogels for enhanced delivery of impermeable anticancer peptides." Biomaterials Science 8, no. 21 (2020): 6100. http://dx.doi.org/10.1039/d0bm90081h.

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Correction for ‘Melittin-encapsulating peptide hydrogels for enhanced delivery of impermeable anticancer peptides’ by Jue-Ping Feng et al., Biomater. Sci., 2020, 8, 4559–4569, DOI: 10.1039/C9BM02080B.

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Chantawannakul, Jarinyagon, Paninnuch Chatpattanasiri, Vichugorn Wattayagorn, Mesayamas Kongsema, Tipanart Noikaew, and Pramote Chumnanpuen. "Virtual Screening for Biomimetic Anti-Cancer Peptides from Cordyceps militaris Putative Pepsinized Peptidome and Validation on Colon Cancer Cell Line." Molecules 26, no. 19 (2021): 5767. http://dx.doi.org/10.3390/molecules26195767.

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Colorectal cancer is one of the leading causes of cancer-related death in Thailand and many other countries. The standard practice for curing this cancer is surgery with an adjuvant chemotherapy treatment. However, the unfavorable side effects of chemotherapeutic drugs are undeniable. Recently, protein hydrolysates and anticancer peptides have become popular alternative options for colon cancer treatment. Therefore, we aimed to screen and select the anticancer peptide candidates from the in silico pepsin hydrolysate of a Cordyceps militaris (CM) proteome using machine-learning-based prediction servers for anticancer prediction, i.e., AntiCP, iACP, and MLACP. The selected CM-anticancer peptide candidates could be an alternative treatment or co-treatment agent for colorectal cancer, reducing the use of chemotherapeutic drugs. To ensure the anticancer properties, an in vitro assay was performed with “CM-biomimetic peptides” on the non-metastatic colon cancer cell line (HT-29). According to the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay results from peptide candidate treatments at 0–400 µM, the IC50 doses of the CM-biomimetic peptide with no toxic and cancer-cell-penetrating ability, original C. militaris biomimetic peptide (C-ori), against the HT-29 cell line were 114.9 µM at 72 hours. The effects of C-ori compared to the doxorubicin, a conventional chemotherapeutic drug for colon cancer treatment, and the combination effects of both the CM-anticancer peptide and doxorubicin were observed. The results showed that C-ori increased the overall efficiency in the combination treatment with doxorubicin. According to the acridine orange/propidium iodine (AO/PI) staining assay, C-ori can induce apoptosis in HT-29 cells significantly, confirmed by chromatin condensation, membrane blebbing, apoptotic bodies, and late apoptosis which were observed under a fluorescence microscope.

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Janin, Y. L. "Peptides with anticancer use or potential." Amino Acids 25, no. 1 (2003): 1–40. http://dx.doi.org/10.1007/s00726-002-0349-x.

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Karbalaeemohammad, Shahrbanoo, and Hossein Naderi-Manesh. "Two Novel Anticancer Peptides from Aurein1.2." International Journal of Peptide Research and Therapeutics 17, no. 3 (2011): 159–64. http://dx.doi.org/10.1007/s10989-011-9253-0.

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Sharma, Ravi D., Jainendra Jain, and Ratan L. Khosa. "Design, Synthesis and Anticancer Activity of Site Specific Short Chain Cationic Peptide." Current Drug Discovery Technologies 17, no. 5 (2020): 631–46. http://dx.doi.org/10.2174/1570163816666190402121033.

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Background: In spite of current progress in treatment methods, cancer is a major source of morbidity and death rate all over the world. Traditional chemotherapeutic agents aim to divide cancerous cells, are often associated with deleterious side effects to healthy cells and tissues. Host defense peptides Cecropin A and B obtained from insects are capable to lyses various types of human cancer cells at peptide concentrations which are not fatal to normal eukaryotic cells. Methods: In the present work we have designed short chain α-helical linear and cyclic peptide from cecropin A having same cationic charge, hydrophobicity and helicity. Synthesis of designed novel short chain linear (10) and cyclic compound (12) was accomplished by using solution phase method. All the coupling reactions were carried out by using dicyclohexylcarbodiimide (DCC) as the coupling reagent at room temperature in the presence of N-methylmorpholine (NMM) as the base. The Structure of newly synthesized peptidse were elucidated by 1H-NMR, 13C-NMR, FT-IR, FABMS and elemental analysis data.Cytotoxicity of synthesized compound was tested against Dalton’s Lymphoma Ascites (DLA), Ehrlich’s Ascites Carcinoma (EAC) and MCF-7 cell lines by using MTT assay and 5-FU as reference compound. Results: From biological assessment,it was found that short chain cyclicpeptide12 showed high level of cytotoxic activity against DLA and EAC cell lines. Conclusion: By utilizing a structure-based rational approach to anticancer peptide design from cecropin A, we were able to develop short chain linear and cyclic peptides having same charge, hydrophobicity and with improved activity. Systematically removing amino acids, we were able to retaining peptide charge and hydrophobicity/hydrophilicity in linear and cyclic peptide which results to optimize the anticancer activity against DLA and EAC cell lines.

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Zhang, Qi-Ting, Ze-Dong Liu, Ze Wang, et al. "Recent Advances in Small Peptides of Marine Origin in Cancer Therapy." Marine Drugs 19, no. 2 (2021): 115. http://dx.doi.org/10.3390/md19020115.

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Cancer is one of the leading causes of death in the world, and antineoplastic drug research continues to be a major field in medicine development. The marine milieu has thousands of biological species that are a valuable source of novel functional proteins and peptides, which have been used in the treatment of many diseases, including cancer. In contrast with proteins and polypeptides, small peptides (with a molecular weight of less than 1000 Da) have overwhelming advantages, such as preferential and fast absorption, which can decrease the burden on human gastrointestinal function. Besides, these peptides are only connected by a few peptide bonds, and their small molecular weight makes it easy to modify and synthesize them. Specifically, small peptides can deliver nutrients and drugs to cells and tissues in the body. These characteristics make them stand out in relation to targeted drug therapy. Nowadays, the anticancer mechanisms of the small marine peptides are still largely not well understood; however, several marine peptides have been applied in preclinical treatment. This paper highlights the anticancer linear and cyclic small peptides in marine resources and presents a review of peptides and the derivatives and their mechanisms.

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Wootton, Christopher A., Carlos Sanchez-Cano, Andrea F. Lopez-Clavijo, et al. "Sequence-dependent attack on peptides by photoactivated platinum anticancer complexes." Chemical Science 9, no. 10 (2018): 2733–39. http://dx.doi.org/10.1039/c7sc05135b.

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Octahedral anticancer platinum(iv) complexes such as trans,trans,trans-[Pt(N<sub>3</sub>)<sub>2</sub>(OH)<sub>2</sub>(pyridine)<sub>2</sub>] (1) can target peptides (and proteins) by sequence-dependent platination and radical mechanisms when activated by UVA or visible light; the specific products are highly dependent on their amino acid composition of the peptide.

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Wu, Qihui, Hanzhong Ke, Dongli Li, Qi Wang, Jiansong Fang, and Jingwei Zhou. "Recent Progress in Machine Learning-based Prediction of Peptide Activity for Drug Discovery." Current Topics in Medicinal Chemistry 19, no. 1 (2019): 4–16. http://dx.doi.org/10.2174/1568026619666190122151634.

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Over the past decades, peptide as a therapeutic candidate has received increasing attention in drug discovery, especially for antimicrobial peptides (AMPs), anticancer peptides (ACPs) and antiinflammatory peptides (AIPs). It is considered that the peptides can regulate various complex diseases which are previously untouchable. In recent years, the critical problem of antimicrobial resistance drives the pharmaceutical industry to look for new therapeutic agents. Compared to organic small drugs, peptide- based therapy exhibits high specificity and minimal toxicity. Thus, peptides are widely recruited in the design and discovery of new potent drugs. Currently, large-scale screening of peptide activity with traditional approaches is costly, time-consuming and labor-intensive. Hence, in silico methods, mainly machine learning approaches, for their accuracy and effectiveness, have been introduced to predict the peptide activity. In this review, we document the recent progress in machine learning-based prediction of peptides which will be of great benefit to the discovery of potential active AMPs, ACPs and AIPs.

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Zhao, Yuhong, Shijing Wang, Wenyi Fei, et al. "Prediction of Anticancer Peptides with High Efficacy and Low Toxicity by Hybrid Model Based on 3D Structure of Peptides." International Journal of Molecular Sciences 22, no. 11 (2021): 5630. http://dx.doi.org/10.3390/ijms22115630.

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Recently, anticancer peptides (ACPs) have emerged as unique and promising therapeutic agents for cancer treatment compared with antibody and small molecule drugs. In addition to experimental methods of ACPs discovery, it is also necessary to develop accurate machine learning models for ACP prediction. In this study, features were extracted from the three-dimensional (3D) structure of peptides to develop the model, compared to most of the previous computational models, which are based on sequence information. In order to develop ACPs with more potency, more selectivity and less toxicity, the model for predicting ACPs, hemolytic peptides and toxic peptides were established by peptides 3D structure separately. Multiple datasets were collected according to whether the peptide sequence was chemically modified. After feature extraction and screening, diverse algorithms were used to build the model. Twelve models with excellent performance (Acc > 90%) in the ACPs mixed datasets were used to form a hybrid model to predict the candidate ACPs, and then the optimal model of hemolytic peptides (Acc = 73.68%) and toxic peptides (Acc = 85.5%) was used for safety prediction. Novel ACPs were found by using those models, and five peptides were randomly selected to determine their anticancer activity and toxic side effects in vitro experiments.

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Guzmán-Rodríguez, Jaquelina Julia, Alejandra Ochoa-Zarzosa, Rodolfo López-Gómez, and Joel E. López-Meza. "Plant Antimicrobial Peptides as Potential Anticancer Agents." BioMed Research International 2015 (2015): 1–11. http://dx.doi.org/10.1155/2015/735087.

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Antimicrobial peptides (AMPs) are part of the innate immune defense mechanism of many organisms and are promising candidates to treat infections caused by pathogenic bacteria to animals and humans. AMPs also display anticancer activities because of their ability to inactivate a wide range of cancer cells. Cancer remains a cause of high morbidity and mortality worldwide. Therefore, the development of methods for its control is desirable. Attractive alternatives include plant AMP thionins, defensins, and cyclotides, which have anticancer activities. Here, we provide an overview of plant AMPs anticancer activities, with an emphasis on their mode of action, their selectivity, and their efficacy.

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Mehrotra, Neha, Surender Kharbanda, and Harpal Singh. "Peptide-based combination nanoformulations for cancer therapy." Nanomedicine 15, no. 22 (2020): 2201–17. http://dx.doi.org/10.2217/nnm-2020-0220.

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Research in cancer therapy is moving towards the use of biomolecules in combination with conventional approaches for improved disease outcome. Among the biomolecules explored, peptides are strong contenders due to their small size, high specificity, low systemic toxicity and wide inter/intracellular targets. The use of nanoformulations for such combination approaches can lead to further improvement in efficacy by reducing off-target cytotoxicity, increasing circulation time, tumor penetration and accumulation. This review focuses on nanodelivery systems for peptide-based combinations with chemo, immuno, radiation and hormone therapy. It gives an overview of the latest therapeutic research being conducted using combination nanoformulations with anticancer peptides, cell penetrating/tumor targeting peptides, peptide nanocarriers, peptidomimetics, peptide-based hormones and peptide vaccines. The challenges hindering clinical translation are also discussed.

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Wang, Yicun, Shuohui Gao, Jiayin Lv, Yang Lin, Li Zhou, and Liying Han. "Phage Display Technology and its Applications in Cancer Immunotherapy." Anti-Cancer Agents in Medicinal Chemistry 19, no. 2 (2019): 229–35. http://dx.doi.org/10.2174/1871520618666181029140814.

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Background:Phage display is an effective technology for generation and selection targeting protein for a variety of purpose, which is based on a direct linkage between the displayed protein and the DNA sequence encoding it and utilized in selecting peptides, improving peptides affinity and indicating protein-protein interactions. Phage particles displaying peptide have the potential to apply in the identification of cell-specific targeting molecules, identification of cancer cell surface biomarkers, identification anti-cancer peptide, and the design of peptide-based anticancer therapy.Method/Results:Literature searches, reviews and assessments about Phage were performed in this review from PubMed and Medline databases.Conclusion:The phage display technology is an inexpensive method for expressing exogenous peptides, generating unique peptides that bind any given target and investigating protein-protein interactions. Due to the powerful ability to insert exogenous gene and display exogenous peptides on the surface, phages may represent a powerful peptide delivery system that can be utilized to develop rapid, efficient, safe and inexpensive cancer therapy methods.

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Jabeen, Farukh, Siva S. Panda, Tamara P. Kondratyuk, et al. "Synthesis, molecular docking and anticancer studies of peptides and iso-peptides." Bioorganic & Medicinal Chemistry Letters 25, no. 15 (2015): 2980–84. http://dx.doi.org/10.1016/j.bmcl.2015.05.020.

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S. Liberio, M., G. A. Joanitti, W. Fontes, and M. S. Castro. "Anticancer Peptides and Proteins: A Panoramic View." Protein & Peptide Letters 20, no. 4 (2013): 380–91. http://dx.doi.org/10.2174/092986613805290435.

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S. Liberio, M., G. A. Joanitti, W. Fontes, and M. S. Castro. "Anticancer Peptides and Proteins: A Panoramic View." Protein & Peptide Letters 20, no. 4 (2013): 380–91. http://dx.doi.org/10.2174/0929866511320040002.

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Raucher, Drazen, and Jung Su Ryu. "Cell-penetrating peptides: strategies for anticancer treatment." Trends in Molecular Medicine 21, no. 9 (2015): 560–70. http://dx.doi.org/10.1016/j.molmed.2015.06.005.

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Karpiński, Tomasz, and Artur Adamczak. "Anticancer Activity of Bacterial Proteins and Peptides." Pharmaceutics 10, no. 2 (2018): 54. http://dx.doi.org/10.3390/pharmaceutics10020054.

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Prabhu, Saurabh, Sarah R. Dennison, Bob Lea, et al. "Anionic Antimicrobial and Anticancer Peptides from Plants." Critical Reviews in Plant Sciences 32, no. 5 (2013): 303–20. http://dx.doi.org/10.1080/07352689.2013.773238.

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Li, Xuan Liu and Yi. "Mechanism of Anticancer Effects of Antimicrobial Peptides." Journal of Fiber Bioengineering and Informatics 8, no. 1 (2015): 25–36. http://dx.doi.org/10.3993/jfbi03201503.

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Grisoni, Francesca, Claudia S. Neuhaus, Gisela Gabernet, Alex T. Müller, Jan A. Hiss, and Gisbert Schneider. "Designing Anticancer Peptides by Constructive Machine Learning." ChemMedChem 13, no. 13 (2018): 1300–1302. http://dx.doi.org/10.1002/cmdc.201800204.

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Aluri, Suhaas, Siti M. Janib, and J. Andrew Mackay. "Environmentally responsive peptides as anticancer drug carriers☆." Advanced Drug Delivery Reviews 61, no. 11 (2009): 940–52. http://dx.doi.org/10.1016/j.addr.2009.07.002.

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Ganesan, Sai Janani, Joel P. Schneider, Robert Blumenthal, and Silvina Matysiak. "Characterization of Anticancer Peptides in Membrane Disruption." Biophysical Journal 104, no. 2 (2013): 597a. http://dx.doi.org/10.1016/j.bpj.2012.11.3314.

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Hoskin, David W., and Ayyalusamy Ramamoorthy. "Studies on anticancer activities of antimicrobial peptides." Biochimica et Biophysica Acta (BBA) - Biomembranes 1778, no. 2 (2008): 357–75. http://dx.doi.org/10.1016/j.bbamem.2007.11.008.

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Teng, Qiu-Xu, Xiaofang Luo, Zi-Ning Lei, et al. "The Multidrug Resistance-Reversing Activity of a Novel Antimicrobial Peptide." Cancers 12, no. 7 (2020): 1963. http://dx.doi.org/10.3390/cancers12071963.

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The overexpression of ATP-binding cassette (ABC) transporters is a common cause of multidrug resistance (MDR) in cancers. The intracellular drug concentration of cancer cells can be decreased relative to their normal cell counterparts due to increased expression of ABC transporters acting as efflux pumps of anticancer drugs. Over the past decades, antimicrobial peptides have been investigated as a new generation of anticancer drugs and some of them were reported to have interactions with ABC transporters. In this article, we investigated several novel antimicrobial peptides to see if they could sensitize ABCB1-overexpressing cells to the anticancer drugs paclitaxel and doxorubicin, which are transported by ABCB1. It was found that peptide XH-14C increased the intracellular accumulation of ABCB1 substrate paclitaxel, which demonstrated that XH-14C could reverse ABCB1-mediated MDR. Furthermore, XH-14C could stimulate the ATPase activity of ABCB1 and the molecular dynamic simulation revealed a stable binding pose of XH-14C-ABCB1 complex. There was no change on the expression level or the location of ABCB1 transporter with the treatment of XH-14C. Our results suggest that XH-14C in combination with conventional anticancer agents could be used as a novel strategy for cancer treatment.

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Huang, Yibing, Qi Feng, Qiuyan Yan, Xueyu Hao, and Yuxin Chen. "Alpha-Helical Cationic Anticancer Peptides: A Promising Candidate for Novel Anticancer Drugs." Mini-Reviews in Medicinal Chemistry 15, no. 1 (2015): 73–81. http://dx.doi.org/10.2174/1389557514666141107120954.

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Wong, Daniel Yuan Qiang, Jun Han Lim, and Wee Han Ang. "Induction of targeted necrosis with HER2-targeted platinum(iv) anticancer prodrugs." Chemical Science 6, no. 5 (2015): 3051–56. http://dx.doi.org/10.1039/c5sc00015g.

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Platinum(iv) prodrug complexes based on the cisplatin/oxaliplatin pharmacophore, containing anti-HER2/neu targeting peptides, were designed to deliver their cytotoxic platinum(ii) payload selectively to highly HER2-expressing cells. Through induction of necrotic cell death, these platinum(iv)–peptide conjugates can circumvent apoptosis-resistance pathways in targeted HER2-positive cells.

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Kardani, Kimia, and Azam Bolhassani. "Antimicrobial/anticancer peptides: bioactive molecules and therapeutic agents." Immunotherapy 13, no. 8 (2021): 669–84. http://dx.doi.org/10.2217/imt-2020-0312.

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Antimicrobial peptides (AMPs) have been known as host-defense peptides. These cationic and amphipathic peptides are relatively short (∼5–50 L-amino acids) with molecular weight less than 10 kDa. AMPs have various roles including immunomodulatory, angiogenic and antitumor activities. Anticancer peptides (ACPs) are a main subset of AMPs as a novel therapeutic approach against tumor cells. The physicochemical properties of the ACPs influence their cell penetration, stability and efficiency of targeting. Up to now, several databases and web servers for in silico prediction of AMPs/ACPs have been established prior to the lab analysis. The present review focuses on the recent advancement about AMPs/ACPs activities including their in silico prediction by computational tools and their potential applications as therapeutic agents especially in cancer.

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Wang, Hua, Ya-Qiong Yan, Yu Yi, et al. "Supramolecular Peptide Therapeutics: Host–Guest Interaction-Assisted Systemic Delivery of Anticancer Peptides." CCS Chemistry 2, no. 6 (2020): 739–48. http://dx.doi.org/10.31635/ccschem.020.202000283.

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Kotamraju, Venkata Ramana, Shweta Sharma, Poornima Kolhar, Lilach Agemy, James Pavlovich, and Erkki Ruoslahti. "Increasing Tumor Accessibility with Conjugatable Disulfide-Bridged Tumor-Penetrating Peptides for Cancer Diagnosis and Treatment." Breast Cancer: Basic and Clinical Research 9s2 (January 2015): BCBCR.S29426. http://dx.doi.org/10.4137/bcbcr.s29426.

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Tumor-homing peptides with tissue-penetrating properties increase the efficacy of targeted cancer therapy by delivering an anticancer agent to the tumor interior. LyP-1 (CGNKRTRGC) and iRGD (CRGDKGPDC) are founding members of this class of peptides. The presence of the cysteines forming the cyclizing disulfide bond complicates conjugation of these peptides with other molecules, such as drugs. Here, we report the synthesis of conjugatable disulfide-bridged peptides and their conjugation to biologically important molecules. We have synthesized the LyP-1, iRGD, and CRGDC (GACRGDCLGA) peptides with a cysteine or maleimidohexanoic acid added externally at N-terminus of the sequences. Subsequent conjugation to payloads yielded stable compounds in which the tumor-homing properties of the peptide and the biological activity of the payload were retained.

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Jeyamogan, Shareni, Naveed A. Khan, Kuppusamy Sagathevan, and Ruqaiyyah Siddiqui. "Anticancer Properties of Asian Water Monitor Lizard (Varanus salvator), Python (Malayopython reticulatus) and Tortoise (Cuora kamaroma amboinensis)." Anti-Cancer Agents in Medicinal Chemistry 20, no. 13 (2020): 1558–70. http://dx.doi.org/10.2174/1871520620666200504103056.

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Background: Cancer contributes to significant morbidity and mortality despite advances in treatment and supportive care. There is a need for the identification of effective anticancer agents. Reptiles such as tortoise, python, and water monitor lizards are exposed to heavy metals, tolerate high levels of radiation, feed on rotten/germ-infested feed, thrive in unsanitary habitat and yet have prolonged lifespans. Such species are rarely reported to develop cancer, suggesting the presence of anticancer molecules/mechanisms. Methods: Here, we tested effects from sera of Asian water monitor lizard (Varanus salvator), python (Malayopython reticulatus) and tortoise (Cuora kamaroma amboinensis) against cancer cells. Sera were collected and cytotoxicity assays were performed using prostate cancer cells (PC3), Henrietta Lacks cervical adenocarcinoma cells (HeLa) and human breast adenocarcinoma cells (MCF7), as well as human keratinized skin cells (Hacat), by measuring lactate dehydrogenase release as an indicator for cell death. Growth inhibition assays were performed to determine the effects on cancer cell proliferation. Liquid chromatography mass spectrometry was performed for molecular identification. Results: The findings revealed that reptilian sera, but not bovine serum, abolished viability of Hela, PC3 and MCF7 cells. Samples were subjected to liquid chromatography mass spectrometry, which detected 57 molecules from V. salvator, 81 molecules from Malayopython reticulatus and 33 molecules from C. kamaroma amboinensis and putatively identified 9 molecules from V. salvator, 20 molecules from Malayopython reticulatus and 9 molecules from C. kamaroma amboinensis when matched against METLIN database. Based on peptide amino acid composition, binary profile, dipeptide composition and pseudo-amino acid composition, 123 potential Anticancer Peptides (ACPs) were identified from 883 peptides from V. salvator, 306 potential ACPs from 1074 peptides from Malayopython reticulatus and 235 potential ACPs from 885 peptides from C. kamaroma amboinensis. Conclusion: To our knowledge, for the first time, we reported comprehensive analyses of selected reptiles’ sera using liquid chromatography mass spectrometry, leading to the identification of potentially novel anticancer agents. We hope that the discovery of molecules from these animals will pave the way for the rational development of new anticancer agents.

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