Version 1
: Received: 4 September 2023 / Approved: 5 September 2023 / Online: 5 September 2023 (04:38:19 CEST)
How to cite:
Outman, A.; Bouhrim, M.; Hountondji, C.; Noman, O.M.; Alqahtani, A.S.; Gressier, B.; Nedjar, N.; Eto, B. Obtaining New Candidate Peptides for Biological Anticancer Drugs from Enzymatic Hydrolysis of Human and Bovine Hemoglobin. Preprints2023, 2023090231. https://doi.org/10.20944/preprints202309.0231.v1
Outman, A.; Bouhrim, M.; Hountondji, C.; Noman, O.M.; Alqahtani, A.S.; Gressier, B.; Nedjar, N.; Eto, B. Obtaining New Candidate Peptides for Biological Anticancer Drugs from Enzymatic Hydrolysis of Human and Bovine Hemoglobin. Preprints 2023, 2023090231. https://doi.org/10.20944/preprints202309.0231.v1
Outman, A.; Bouhrim, M.; Hountondji, C.; Noman, O.M.; Alqahtani, A.S.; Gressier, B.; Nedjar, N.; Eto, B. Obtaining New Candidate Peptides for Biological Anticancer Drugs from Enzymatic Hydrolysis of Human and Bovine Hemoglobin. Preprints2023, 2023090231. https://doi.org/10.20944/preprints202309.0231.v1
APA Style
Outman, A., Bouhrim, M., Hountondji, C., Noman, O.M., Alqahtani, A.S., Gressier, B., Nedjar, N., & Eto, B. (2023). Obtaining New Candidate Peptides for Biological Anticancer Drugs from Enzymatic Hydrolysis of Human and Bovine Hemoglobin. Preprints. https://doi.org/10.20944/preprints202309.0231.v1
Chicago/Turabian Style
Outman, A., Naïma Nedjar and Bruno Eto. 2023 "Obtaining New Candidate Peptides for Biological Anticancer Drugs from Enzymatic Hydrolysis of Human and Bovine Hemoglobin" Preprints. https://doi.org/10.20944/preprints202309.0231.v1
Abstract
Enzymatic hydrolysis of bovine and human hemoglobin yields a diversity of bioactive peptides, some of which are recognized for their antimicrobial properties. Certain small antimicrobial and anticancer peptides target protein synthesis inhibition. This study aims to produce bioactive peptides through enzymatic hemoglobin hydrolysis and evaluate their effects on cell growth inhibition, potentially serving as candidates for biological anticancer drugs. Rapid screening of candidate anticancer peptides derived from enzymatic hydrolysis of bovine and human hemoglobin was conducted using the Lepidium sativum radicle growth technique. The results demonstrate that: 1) the degree of hydrolysis (DH) significantly influences the production of bioactive peptides. DH levels of 3-10% yield considerably stronger radicle growth inhibition compared to DH 0 (native hemoglobin form), exhibiting three to four times greater intensity. 2) Certain peptide fractions from bovine hemoglobin exhibit higher activity than those from human hemoglobin. 3) The structural characteristics of peptides play a crucial role in the observed biological effects. 4) The α137-141 peptide is the most active among the fractions obtained from bovine (IC50 = 29 ± 1 µg/mL) and human hemoglobin (IC50 = 48 ± 2 µg/mL), standing out 10 to 15 times more potent than other hemoglobin fractions. In conclusion, these findings affirm the bioactivity of peptide fractions obtained from bovine and human hemoglobin. The study highlights how enzymatic hydrolysis of bovine and human hemoglobin can yield peptides that inhibit protein synthesis. Ultimately, these results suggest the feasibility of obtaining candidate peptides for biological anticancer drugs from both human and bovine hemoglobin sources. These scientific advances show new hope in the fight against cancer which affects a large number of people around the world.
Keywords
human hemoglobin; bovine hemoglobin bovine; enzymatic hydrolysis; bioactive peptides; medicine candidate anticancer; Screening
Subject
Medicine and Pharmacology, Pharmacology and Toxicology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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