Enzymatic Hydrolyzed Feather Peptide, a Welcoming Drug for Multiple-Antibiotic-Resistant Staphylococcus aureus: Structural Analysis and Characterization
| Autor: | Arpan Das, Ahmet Kati, Bikas R. Pati, Santi M. Mandal, Suman Kumar Maji, Keshab Chandra Mondal, Amit Kumar Mandal, Kuntal Ghosh, Arpita Mandal, Pradeep Kumar Das Mohapatra, Tanmay Paul, Suman Kumar Halder |
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| Rok vydání: | 2015 |
| Předmět: |
Methicillin-Resistant Staphylococcus aureus
Bioengineering Peptide Microbial Sensitivity Tests Biology medicine.disease_cause Staphylococcal infections Applied Microbiology and Biotechnology Biochemistry Microbiology Cell wall Minimum inhibitory concentration Drug Resistance Bacterial medicine Animals Humans Mode of action Molecular Biology Chromatography High Pressure Liquid chemistry.chemical_classification Minimum bactericidal concentration General Medicine Feathers Staphylococcal Infections medicine.disease Enzyme chemistry Staphylococcus aureus Peptides Chickens Biotechnology |
| Zdroj: | Applied Biochemistry and Biotechnology. 175:3371-3386 |
| ISSN: | 1559-0291 0273-2289 |
| DOI: | 10.1007/s12010-015-1509-2 |
| Popis: | This study aimed to explore the bactericidal activity of a feather-degraded active peptide against multiple-antibiotic-resistant (MAR) Staphylococcus aureus. An antibacterial peptide (ABP) was isolated from the chicken feathers containing fermented media of Paenibacillus woosongensis TKB2, a keratinolytic soil isolate. It was purified by HPLC, and its mass was found to be 4666.87 Da using matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) spectroscopy. The minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) values of this peptide were 22.5 and 90 μg/ml, respectively. SEM study revealed the distorted cell wall of the test strain along with pore formation. The possible reason for bactericidal activity of the peptide is due to generation of reactive oxygen species (ROS), resulting in membrane damage and leakage of intracellular protein. Complete sequence of the peptide was predicted and retrieved from the sequence database of chicken feather keratin after in silico trypsin digestion using ExPASy tools. Further, net charge, hydrophobicity (77.7 %) and molecular modelling of the peptide were evaluated for better understanding of its mode of action. The hydrophobic region (17 to 27) of the peptide may facilitate for initial attachment on the bacterial membrane. The ABP exhibited no adverse effects on RBC membrane and HT-29 human cell line. This cytosafe peptide can be exploited as an effective therapeutic agent to combat Staphylococcal infections. |
| Databáze: | OpenAIRE |
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