This study aimed to explore the bactericidal activity of a feather-degraded active peptide agains... more 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 exhibitedno 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.
INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY (IJSEM)
A Gram positive, rod shaped, facultatively oligotrophic bacterial strain, designated MB18T, was i... more A Gram positive, rod shaped, facultatively oligotrophic bacterial strain, designated MB18T, was isolated from a water sample collected from River Mahananda at Siliguri (26°44'23.20"N, 88°25'22.89"E), West Bengal, India. On the basis of 16S rRNA gene sequence similarity, the closest relative of this strain was Brevibacterium epidermidis NCDO 2286T (96% similarity). The DNA G+C content of strain MB18T was 64.6 mol%. Chemotaxonomic data [Mk-8(H2) as major major menaquinone, galac-tose as sole cell wall sugar, meso-diaminopimelic acid as diagnostic cell wall diamino acid, phosphatidylglycerol (PG) and diphosphatidylglycerol (DPG) as constituents of polar lipids, anteiso-C15: 0 , anteiso-C17: 0 and iso-C15:0 as the major fatty acids] supported the affiliation of strain MB18T to the genus Brevibacterium. The results of DNA G + C content, 16S rRNA gene sequence analysis, biochemical and physiological analyses allowed genotypic and phenotypic differentiation of strain MB18T from its nearest neighbour B. epidermidis. The isolate, therefore represents a new species, for which the name Brevibacterium siliguriense sp. nov. is proposed, with the type strain is MB18T (=DSM 23676T = LMG 25772T).
This study aimed to explore the bactericidal activity of a feather-degraded active peptide agains... more 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 exhibitedno 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.
INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY (IJSEM)
A Gram positive, rod shaped, facultatively oligotrophic bacterial strain, designated MB18T, was i... more A Gram positive, rod shaped, facultatively oligotrophic bacterial strain, designated MB18T, was isolated from a water sample collected from River Mahananda at Siliguri (26°44'23.20"N, 88°25'22.89"E), West Bengal, India. On the basis of 16S rRNA gene sequence similarity, the closest relative of this strain was Brevibacterium epidermidis NCDO 2286T (96% similarity). The DNA G+C content of strain MB18T was 64.6 mol%. Chemotaxonomic data [Mk-8(H2) as major major menaquinone, galac-tose as sole cell wall sugar, meso-diaminopimelic acid as diagnostic cell wall diamino acid, phosphatidylglycerol (PG) and diphosphatidylglycerol (DPG) as constituents of polar lipids, anteiso-C15: 0 , anteiso-C17: 0 and iso-C15:0 as the major fatty acids] supported the affiliation of strain MB18T to the genus Brevibacterium. The results of DNA G + C content, 16S rRNA gene sequence analysis, biochemical and physiological analyses allowed genotypic and phenotypic differentiation of strain MB18T from its nearest neighbour B. epidermidis. The isolate, therefore represents a new species, for which the name Brevibacterium siliguriense sp. nov. is proposed, with the type strain is MB18T (=DSM 23676T = LMG 25772T).
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Papers by AHMET KATI
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 exhibitedno 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.
Conference Presentations by AHMET KATI
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 exhibitedno 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.