SavedAdd your journal

Journals / Türk Biyokimya Dergisi / 2019 / Cilt: 44 - Sayı: 5

Investigation and isolation of peptide based antiglycating agents from various sources

Çeşitli Kaynaklardan Peptid Temelli Antiglikasyon Ajanlarının İzolasyonu ve Araştırılması

Figen ZİHNİOĞLU
Hatice K. KANİ
Ebru K. KOCAZORBAZ
Pages
699–705
Publication Date
2022-11-05
DOI
—
🏛️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)

Among all plant peptide isolates soybean was found to be most efficient by meansof antiglycating (IC50 1.33 μg/mL), antioxidant (28.2 ± 1.4 μmol AAE/mg) and metal chelation activity (55%).Conclusion: As a result, this study can provide preliminary data to literature to support researches those focused on peptide based glycation inhibitors and discovery of potentAGE inhibitory peptides

📌 3 Key Takeaways

🎯
Objective & Hypothesis:AbstractBackground: In this work, peptide based antiglycation agents from various sources against the advanced glycation endproducts (AGE) formation was investigated.Materials and methods: As a source of peptides with deglycating activity, Glycine max, Hordeum vulgare, Triticum aestivum, Avena sativa, Prunus dulcis ve Juglans regia were used.
📊
Key Findings & Data:The metal chelating activity and antioxidant activity were determined by Cu(II) chelating activity and CUPRAC (Cupric Reducing Antioxidant Capacity) methods.
💡
Conclusion & Impact:Among all plant peptide isolates soybean was found to be most efficient by meansof antiglycating (IC50 1.33 μg/mL), antioxidant (28.2 ± 1.4 μmol AAE/mg) and metal chelation activity (55%).Conclusion: As a result, this study can provide preliminary data to literature to support researches those focused on peptide based glycation inhibitors and discovery of potentAGE inhibitory peptides
🔬Design:Modeling & Simulation
📍Scope:Comprehensive Sample
⚙️Variables:Domain Parameters

Abstract

AbstractBackground: In this work, peptide based antiglycation agents from various sources against the advanced glycation endproducts (AGE) formation was investigated.Materials and methods: As a source of peptides with deglycating activity, Glycine max, Hordeum vulgare, Triticum aestivum, Avena sativa, Prunus dulcis ve Juglans regia were used. The metal chelating activity and antioxidant activity were determined by Cu(II) chelating activity and CUPRAC (Cupric Reducing Antioxidant Capacity) methods. Antidiabetic activity was evaluated through BSA-glucose model.Results: Most of the extracts obtained have inhibitory activity against AGE formation. Among all plant peptide isolates soybean was found to be most efficient by meansof antiglycating (IC50 1.33 μg/mL), antioxidant (28.2 ± 1.4 μmol AAE/mg) and metal chelation activity (55%).Conclusion: As a result, this study can provide preliminary data to literature to support researches those focused on peptide based glycation inhibitors and discovery of potentAGE inhibitory peptides

Özet

ÖzAmaç: Bu çalışmada, ileri glikasyon son ürünleri (AGE) ile oluşabilecek protein hasarlarının minimize edilmesi amacı ile çeşitli kaynaklardan antiglikasyon etkinliği olan peptid yapıda bileşiklerin araştırılması hedeflendi.Gereç ve Yöntem: Deglikasyon etkinliği olabilecek endojen peptidlerin eldesinde kaynak olarak Glycine max, Hordeum vulgare, Triticum aestivum, Avena sativa, Prunus dulcis ve Juglans regia kullanıldı. Peptid izolatlarının deglikasyon aktiviteleri BSA-Glukoz modeli ile, antioksidan kapasitesi ve metal bağlama etkinliği ise CUPRAC (bakır(II) iyonu indirgeme antioksidan kapasite) ve bakır şelatasyon metodları kullanılarak incelenmiştir.Bulgular: Çalışılan ekstrakların çoğunda AGE oluşumuna karşı inhibitör aktivitesi gözlendi. İncelenen tüm parametreler açısından değerlendirildiğinde ise soya peptid izolatının en iyi deglikasyon (IC50 1.33 μg/mL), antioksidan (28.2 ± 1.4 μmolAAE/mg) ve metal bağlama etkinliği (% 55) olduğu saptanmış olup daha etkin ve seçimli inhibitörlerin geliştirilmesi açısından önemli olduğu düşünüldü.Sonuç: Sonuç olarak, peptid bazlı glikasyon inhibitörlerinin ve güçlü AGE peptit inhibitörlerin keşfedilmesine yönelik araştırmaları desteklemek için literatürlere katkı sağlayacağı düşünüldü.

🔖

Cite This Article

ZİHNİOĞLU, F., KANİ, H. K., KOCAZORBAZ, E. K. (2022). Investigation and isolation of peptide based antiglycating agents from various sources. Türk Biyokimya Dergisi, Cilt: 44 - Sayı: 5, 699–705. https://ajindex.com/articles/620853

📄 Full Text PDF Viewer

📄

PDF görüntüleyici hazırlanıyor...

References (15)

  1. Altan N. Diabetes mellitus and oxidative stress. Turk J Biochem 2006;31:51–6
  2. Brewer GJ. Risks of copper and iron toxicity during aging in humans. Chem Res Toxicol 2009; 23:319–26
  3. Van Campenhout A, Van Campenhout C, Lagrou AR, Manuel-YKeenoy B. Effects of in vitro glycation on Fe3 + binding and Fe3 + isoforms of transferrin. Clin Chem 2004;50:1640–9
  4. Chen CL, Guangyuan HO. Generation of proline-specific Maillard compounds by the reaction of 2-deoxyglucose with proline. J Agric Food Chem 1997;45:2996–9
  5. Price DL, Rhett PM, Thorpe SR, Baynes JW. Chelating activity of advanced glycation end-product (AGE) inhibitors. J Biol Chem 2001;276:48967–72
  6. Ramonaitytė DT, Keršienė M, Adams A, Tehrani KA, De Kimpe N. The interaction of metal ions with Maillard reaction products in a lactose–glycine model system. Food Res Int 2009;42:331–6
  7. Sattarahmady N, Moosayi-Moyahedi AA, Ahmad F, Hakimelahi GH, Habibi-Rezaei M, Saboury AA, et al. Formation of the molten globule-like state during prolonged glycation of human serum albumin. Biochim Biophys Acta 2007;1770:933–42
  8. Christen Y. Oxidative stress and Alzheimer disease. Am J Clin Nutr 2000;71:621–9
  9. Dukic-Stefanovic S, Schinzel R, Riederer P, Münch G. AGES in brain ageing: age-inhibitors as neuroprotective and anti-dementia drugs? Biogerontology 2001;2:19–34
  10. Nawale RB, Mourya VK, Bhise SB. Non-enzymatic glycation of proteins: a cause for complications in diabetes. Indian J Biochem Biophys 2006;43:337–43
  11. Ardestani A, Yazdanparast R. Cyperus rotundus suppresses AGE formation and protein oxidation in a model of fructose-mediated protein glycoxidation. Int J Biol Macromol 2007;41:572–8
  12. Belia F, Amorini AM, La Mendola D, Vecchio G, Tavazzi B, Giardina B, et al. New glycosidic derivatives of histidinecontaining dipeptides with antioxidant properties and resistant to carnosinase activity. Eur J Med Chem 2008;43:373–80
  13. Brownson C, Hipkiss AR. Carnosine reacts with a glycated protein. Free Radic Biol Med 2000;28:1564–70
  14. Chetyrkin SV, Mathis ME, Ham AJ, Hachey DL, Hudson BG, Voziyan PA. Propagation of protein glycation damage involves modification of tryptophan residues via reactive oxygen species: inhibition by pyridoxamine. Free Radic Biol Med 2008;44:1276–85
  15. Culbertson SM, Vassilenko EI, Morrison LD, Ingold KU. Paradoxical impact of antioxidants on post-amadori glycoxidation: counterintuitive increase in the yields of pentosidine and entosidine and Nε-carboxymethyllysine us