Habibie, Ahmad and Raharjo, Tri Joko and Swasono, Respati Tri and Retnaningrum, Endah (2023) Antibacterial activity of active peptide from marine macroalgae Chondrus crispus protein hydrolysate against Staphylococcus aureus. Pharmacia, 70 (4). 983 – 992. ISSN 04280296
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Abstract
Macroalgae is a protein source with the potential to yield antimicrobial peptides (AMPs) that exhibit a wide range of biological activities. This study aimed to find bioactive peptide-based antibacterial compounds from marine macroalgae Chondrus crispus protein hydrolysate. The peptides were isolated by solid phase extraction with a strong cation exchanger from trypsin-digested and α-chymotrypsin-digested hydrolysates. Certain fractions of the hydrolyzed protein displayed a good inhibition zone, with the α-chymotrypsin- digested fraction eluted at pH 9 exhibiting the highest inhibition against Gram-negative bacteria Staphylococcus aureus. Several peptides were characterized as cationic helical peptides with hydrophobicity percentages of 16.67–77.78. The potential antibacterial peptide P01 KKNVTTLAPLVF was identified as an α-helical cationic antibacterial peptide with 0.525 GRAVY value, amphipathic structure, and +2 total charge. Moreover, strong interaction was observed between P07 SAGSGNEGLSGW and P20 RTASSR peptide with DNA gyrase and DHFR receptors from S. aureus with binding energy -8.0 and -7.3 kcal/mol, respectively. © Copyright Habibie A et al. This is an open access article distributed under the terms of the Creative Commons Attribution License (CC-BY 4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Item Type: | Article |
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Additional Information: | Cited by: 2; All Open Access, Gold Open Access, Green Open Access |
Uncontrolled Keywords: | algal protein; chymotrypsin A; dihydrofolate reductase; DNA topoisomerase (ATP hydrolysing); polypeptide antibiotic agent; protein hydrolysate; streptomycin; trypsin; alpha helix; antibacterial activity; Article; cation exchange; Chondrus crispus; controlled study; drug protein binding; fractionation; hydrolysis; hydrophobicity; molecular docking; nonhuman; protein purification; solid phase extraction; Staphylococcus aureus; zone of inhibition |
Subjects: | Q Science > QD Chemistry |
Divisions: | Faculty of Mathematics and Natural Sciences > Chemistry Department |
Depositing User: | Sri JUNANDI |
Date Deposited: | 30 Oct 2024 01:28 |
Last Modified: | 30 Oct 2024 01:28 |
URI: | https://ir.lib.ugm.ac.id/id/eprint/5998 |