SavedAdd your journal

Journals / Afyon Kocatepe Üniversitesi Fen ve Mühendislik Bilimleri Dergisi / 2026 / Cilt: 26 Sayı: 3

Investigation of in vitro Biological Activities of 2-((6-methylpyridin-2-yl)amino)acetic acid

2-((6-metilpiridin-2-il)amino)asetik asid’in in vitro Biyolojik Aktivitesinin Araştırılması

Merve Balaban(SIIRT UNIVERSITY)0000-0002-4188-1110
Ümit Çalişir(SIIRT UNIVERSITY)0000-0001-7699-2008
Yasemin Camadan(ARTVİN ÇORUH ÜNİVERSİTESİ)0000-0002-9000-7761
Ebru Akkemik(SIIRT UNIVERSITY)0000-0002-4177-4884
Pages
549–557
Publication Date
2026-06-03
🏛️Bibliographic metadata and full text access for this article are provided via DergiPark.
DergiPark Record ↗
✨

AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

It was found that the highest antioxidant activity of 2-((6-methylpyridin-2-yl)amino) acetic acid was 0.0372±0.0018 µg trolox eq./µL by the CUPRAC method.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Peptoids (N-substituted glycine oligomers) are a class of synthetic heteropolymers that can mimic the structures of peptides.
📊
Key Findings & Data:This study investigates the in vitro biological activities and drug potential of the peptoid derivative 2-((6-methylpyridin-2-yl)amino)acetic acid.
💡
Conclusion & Impact:It was found that the highest antioxidant activity of 2-((6-methylpyridin-2-yl)amino) acetic acid was 0.0372±0.0018 µg trolox eq./µL by the CUPRAC method.
🔬Design:Araştırma Makalesi
📍Scope:Comprehensive Sample
⚙️Variables:N-sübstitüe amino asit · Antioksidan · DNA koruma

Abstract

Peptoids (N-substituted glycine oligomers) are a class of synthetic heteropolymers that can mimic the structures of peptides. Due to their potent biological activities, their use as drugs in the medical and health sectors is being investigated. This study investigates the in vitro biological activities and drug potential of the peptoid derivative 2-((6-methylpyridin-2-yl)amino)acetic acid. Antioxidant properties were determined by CUPRAC (Cupric Reducing Antioxidant Capacity), DPPH (2,2-diphenyl-1-picrylhydrazyl) and FRAP (Ferric Reducing Antioxidant Power) methods. DNA protection and DNA damage analyses were performed to determine its effects on plasmid DNA. Finally, it’s in vitro inhibitory activity on the enzyme activities of GST (glutathione s-transferase) and hCA I-II (human carbonic anhydrase I-II), important enzymes of various metabolic pathways, was determined. It was found that the highest antioxidant activity of 2-((6-methylpyridin-2-yl)amino) acetic acid was 0.0372±0.0018 µg trolox eq./µL by the CUPRAC method. While the compound did not cause any damage to DNA in the 0.5-1 mg/mL range, it was found to have a DNA protective effect at a concentration of 0.5 mg/mL. Besides, the best inhibitory effect of the compound was shown to be against hCA I isoenzyme.

Özet

Peptoidler (N-sübstitüe glisin oligomerleri), peptitlerin yapılarını taklit edebilen sentetik heteropolimer sınıfıdır. Güçlü biyolojik aktivitelerinden dolayı tıp ve sağlık sektöründe ilaç olarak kullanımları araştırılmaktadır. Bu çalışma, peptoid türevi 2-((6-metilpiridin-2-il)amino)asetik asidin in vitro biyolojik aktivitelerini ve ilaç potansiyelini araştırmaktadır. CUPRAC (Bakır (II) indirgeyici antioksidan kapasitesi), DPPH (2,2-difenil-1-pikrilhidrazil) ve FRAP (Demir (III) indirgeyici antioksidan kapasite yöntemleri ile antioksidan özelliği belirlendi. Plazmit DNA üzerindeki etkilerini belirlemek için DNA koruma ve DNA hasar analizleri gerçekleştirildi. Son olarak çeşitli metabolik yolakların önemli enzimleri olan GST (glutatyon s-transferaz) ve hCA I-II (human carbonic anhidraz I-II) enzim aktiviteleri üzerindeki in vitro inhibisyon aktivitesi tespit edildi. Yapılan analizler neticesinde 2-((6-metilpiridin-2-il)amino) asetik asid’in en yüksek antioksidan aktivitesi CUPRAC yöntemiyle 0,0372±0,0018 µg troloks ekv./µL olarak hesaplandı. Bileşik 0,5-1 mg/mL aralığında DNA üzerinde bir hasar oluşturmaz iken 0,5 mg/mL konsantrasyonda DNA koruma etkisine sahip olduğu belirlenmiştir. Ayrıca en iyi inhibitör etkisini hCA I izoenzime karşı göstermiştir.

🔖

Cite This Article

Balaban, M., Çalişir, Ü., Camadan, Y., Akkemik, E. (2026). Investigation of in vitro Biological Activities of 2-((6-methylpyridin-2-yl)amino)acetic acid. Afyon Kocatepe Üniversitesi Fen ve Mühendislik Bilimleri Dergisi, Cilt: 26 Sayı: 3, 549–557. https://doi.org/10.35414/akufemubid.1822075

📄 Full Text PDF Viewer

📄

PDF görüntüleyici hazırlanıyor...

References (36)

  1. Adem, S., Akkemik, E., Aksit, H., Guller, P., Tüfekci, A. R., Demirtas, İ., & Ciftci, M. (2019). Activation and inhibition effects of some natural products on human cytosolic CAI and CAII. Medicinal Chemistry Research, 28(5), 711–722. https://doi.org/10.1007/s00044-019-02329-1
  2. Akkemik, E., Aybek, A., & Felek, I. (2019). Effects of Cefan melon (Cucumis melo L.) seed extracts on human erythrocyte carbonic anhydrase I-II enzymes. Applied Ecology & Environmental Research, 17(6). 14699-14713 http://doi.org/10.15666/aeer/1706_1469914713
  3. Akkemik, E., Fidan, M., Balaban, M., & Inal, B. (2022). ICP-OES AND LC-ESI-MS/MS ANALYSES, ENZYME INHIBITION AND DNA PROTECTION POTENTIAL OF PELARGONIUM QUERCETORUM AGNEW. Studia Universitatis Babes-Bolyai, Chemia, 67(4), 197-213. https://doi.org/10.24193/subbchem.2022.4.13
  4. Aksoy, M., Ozaslan, M. S., & Kufrevioglu, O. I. (2016). Purification of glutathione S-transferase from Van Lake fish (Chalcalburnus tarichii Pallas) muscle and investigation of some metal ions effect on enzyme activity. Journal of enzyme inhibition and medicinal chemistry, 31(4), 546–550. https://doi.org/10.3109/14756366.2015.1046063
  5. Apak, R., Güçlü, K., Demirata, B., Özyürek, M., Çelik, S. E., Bektaşoğlu, B., Berker, K. I., & Özyurt, D. (2007). Comparative evaluation of various total antioxidant capacity assays applied to phenolic compounds with the CUPRAC assay. Molecules, 12(7), 1496–1547. https://doi.org/10.3390/12071496
  6. Askin, S., Tahtaci, H., Türkeş, C., Demir, Y., Ece, A., Çiftçi, G. A., & Beydemir, Ş. (2021). Design, synthesis, characterization, in vitro and in silico evaluation of novel imidazo [2, 1-b][1, 3, 4] thiadiazoles as highly potent acetylcholinesterase and non-classical carbonic anhydrase inhibitors. Bioorganic Chemistry, 113, 105009. https://doi.org/10.1016/j.bioorg.2021.105009
  7. Benvenuti, S., Pellati, F., Melegari, M. a., & Bertelli, D. (2004). Polyphenols, anthocyanins, ascorbic acid, and radical scavenging activity of Rubus, Ribes, and Aronia. Journal of food science, 69(3), FCT164–FCT169. https://doi.org/10.1111/j.1365-2621.2004.tb13352.x
  8. Benzie, I. F. (1996). An automated, specific, spectrophotometric method for measuring ascorbic acid in plasma (EFTSA). Clinical biochemistry, 29(2), 111–116. https://doi.org/10.1016/0009-9120(95)02013-6
  9. Benzie, I. F., & Szeto, Y. (1999). Total antioxidant capacity of teas by the ferric reducing/antioxidant power assay. Journal of agricultural and food chemistry, 47(2), 633–636. https://doi.org/10.1021/jf9807768
  10. Caglayan, C., & Gulcin, İ. (2018). The toxicological effects of some avermectins on goat liver carbonic anhydrase enzyme. Journal of biochemical and molecular toxicology, 32(1), e22010. https://doi.org/10.1002/jbt.22010
  11. Çalışır, Ü. (2025). Synthesis and characterization of pyridine-pyrrole-modified carbon nanotube derivatives via ylides. Current Organic Chemistry, 29(2), 153–163. https://doi.org/10.2174/011385272831933624071105314
  12. Çalışır, Ü., & Çiçek, B. (2023). Bazı yeni N-sübstitüe amino asit esterlerinin yapısal özelliklerinin in silico ile araştırılması. Balıkesir Üniversitesi Fen Bilimleri Enstitüsü Dergisi, 25(2), 748–760. https://doi.org/10.25092/baunfbed.1310449
  13. Camadan, Y., Akkemik, E., Güller, P., Ceylan, Ş., & Özdemir, H. (2024). Investigation of the Effects of 1, 2, 4‐Triazole and Thiazole Ring‐Containing Hybrid Molecules on Carbonic Anhydrase I and II. ChemistrySelect, 9(6), e202303236. https://doi.org/10.1002/slct.202303236
  14. Carocho, M., & Ferreira, I. C. (2013). A review on antioxidants, prooxidants and related controversy: Natural and synthetic compounds, screening and analysis methodologies and future perspectives. Food and chemical toxicology, 51, 15–25. http://dx.doi.org/10.1016/j.fct.2012.09.021
  15. Çiftçi, B., Koçak Mutlu, A., & Akkemik, E. (2025). Purification of glutathione S-transferase enzyme from liver tissue of shabout (Barbus grypus Heckel) and investigation of the inhibition effect of some metal ions under in vitro conditions. Fish physiology and biochemistry, 51(1), 28. https://doi.org/10.1007/s10695-024-01424-4
  16. Elchinger, P., Delattre, C., Faure, S., Roy, O., Badel, S., Bernardi, T., Michaud, P., & Taillefumier, C. (2017). Antioxidant activities of peptoid-grafted chitosan films. Applied biochemistry and biotechnology, 181(1), 283–293. https://doi.org/10.1007/s12010-016-2212-7
  17. Hashkavayi, A. B., Hashemnia, S., & Osfouri, S. (2020). Investigations of antioxidant potential and protective effect of Acanthophora algae on DNA damage: An electrochemical approach. Microchemical Journal, 159, 105455. http://doi.org/10.1016/j.microc.2020.105455
  18. Holm, P. J., Morgenstern, R., & Hebert, H. (2002). The 3-D structure of microsomal glutathione transferase 1 at 6 Å resolution as determined by electron crystallography of p22121 crystals. Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, 1594(2), 276–285. http://doi.org/10.1016/s0167-4838(01)00311-9
  19. Karioti, A., Carta, F., & Supuran, C. T. (2016). Phenols and polyphenols as carbonic anhydrase inhibitors. Molecules, 21(12), 1649. http://doi.org/10.3390/molecules21121649
  20. Kırboğa, K. K., & Işık, M. (2024). Explainable artificial intelligence in the design of selective carbonic anhydrase I‐II inhibitors via molecular fingerprinting. Journal of Computational Chemistry, 45(18), 1530–1539. https://doi.org/10.1002/jcc.27335
  21. Lehtonen, J., Shen, B., Vihinen, M., Casini, A., Scozzafava, A., Supuran, C. T., Parkkila, A.-K., Saarnio, J., Kivelä, A. J., & Waheed, A. (2004). Characterization of CA XIII, a novel member of the carbonic anhydrase isozyme family. Journal of Biological Chemistry, 279(4), 2719–2727. http://doi.org/10.1074/jbc.M308984200
  22. Li, C., Chen, L., & Chen, J. (2002). DNA damage induces MDMX nuclear translocation by p53-dependent and-independent mechanisms. Molecular and cellular biology, 22(21), 7562–7571. https://doi.org/10.1128/MCB.22.21.7562-7571.2002
  23. Lomelino, C. L., Supuran, C. T., & McKenna, R. (2016). Non-classical inhibition of carbonic anhydrase. International journal of molecular sciences, 17(7), 1150. https://doi.org/10.3390/ijms17071150.
  24. Mittler, R. (2017). ROS are good. Trends in plant science, 22(1), 11–19. http://doi.org/10.1016/j.tplants.2016.08.002
  25. Phaniendra, A., Jestadi, D. B., & Periyasamy, L. (2015). Free radicals: properties, sources, targets, and their implication in various diseases. Indian journal of clinical biochemistry, 30(1), 11–26. http://doi.org/10.1007/s12291-014-0446-0
  26. Prabhu, K. S., Reddy, P. V., Jones, E. C., Liken, A. D., & Reddy, C. C. (2004). Characterization of a class alpha glutathione-S-transferase with glutathione peroxidase activity in human liver microsomes. Archives of biochemistry and biophysics, 424(1), 72–80. http://doi.org/10.1016/j.abb.2004.02.002
  27. Robertson, E. J., Battigelli, A., Proulx, C., Mannige, R. V., Haxton, T. K., Yun, L., Whitelam, S., & Zuckermann, R. N. (2016). Design, synthesis, assembly, and engineering of peptoid nanosheets. Accounts of Chemical Research, 49(3), 379–389. https://doi.org/10.1021/acs.accounts.5b00439
  28. Shah, P., & Modi, H. (2015). Comparative study of DPPH, ABTS and FRAP assays for determination of antioxidant activity. Int. J. Res. Appl. Sci. Eng. Technol, 3(6), 636–641.
  29. Smirnovienė, J., Smirnovas, V., & Matulis, D. (2017). Picomolar inhibitors of carbonic anhydrase: importance of inhibition and binding assays. Analytical Biochemistry, 522, 61–72. https://doi.org/10.1016/j.ab.2017.01.022
  30. Suwal, S., & Kodadek, T. (2013). Synthesis of libraries of peptidomimetic compounds containing a 2-oxopiperazine unit in the main chain. Organic & biomolecular chemistry, 11(13), 2088–2092. https://doi.org/10.1039/c3ob27476d
  31. Taslimi, P., Kandemir, F. M., Demir, Y., İleritürk, M., Temel, Y., Caglayan, C., & Gulçin, İ. (2019). The antidiabetic and anticholinergic effects of chrysin on cyclophosphamide‐induced multiple organ toxicity in rats: Pharmacological evaluation of some metabolic enzyme activities. Journal of biochemical and molecular toxicology, 33(6), e22313. https://doi.org/10.1002/jbt.22313
  32. Verpoorte, J. A., Mehta, S., & Edsall, J. T. (1967). Esterase activities of human carbonic anhydrases B and C. Journal of Biological Chemistry, 242(18), 4221–4229. https://doi.org/10.1016/S0021-9258(18)95800-X
  33. Wang, X. C., Yong, H. M., Gao, L., Li, L. L., Jin, M. J., & Liu, J. (2019). Preparation and characterization of antioxidant and pH-sensitive films based on chitosan and black soybean seed coat extract. Food Hydrocolloids, 89, 56–66. https://doi.org/10.1016/j.foodhyd.2018.10.019
  34. Xu, B., Dong, Q., Yu, C., Chen, H., Zhao, Y., Zhang, B., Yu, P., & Chen, M. (2024). Advances in research on the activity evaluation, mechanism and structure-activity relationships of natural antioxidant peptides. Antioxidants, 13(4), 479. https://doi.org/10.3390/antiox13040479
  35. Yoo, B., & Kirshenbaum, K. (2008). Peptoid architectures: elaboration, actuation, and application. Current opinion in chemical biology, 12(6), 714–721. https:/doi.org/10.1016/j.cbpa.2008.08.015
  36. Zuckermann, R. N. (2011). Peptoid origins. Peptide Science, 96(5), 545–555. https://doi.org/10.1002/bip.21573