Characterization of the novel antibacterial peptide Leucrocin from crocodile (Crocodylus siamensis) white blood cell extracts

Pata, Supawadee; Yaraksa, Nualyai; Daduang, Sakda; Temsiripong, Yosapong; Svasti, Jisnuson; Araki, Toshimitsu; Thammasirirak, Sompong

doi:10.1016/j.dci.2010.12.011

Cited by 83 publications

(71 citation statements)

References 41 publications

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“…However, there were contained random coils and extended strands. From the results, it is possible due to these peptides might adopt a helical structure from a random coil while their interaction with membranes [7,29,31,33]. Moreover, peptides a (V1-V13), (K16-A26) and b (A69-S80) are not contain positively charged amino acids but have high hydrophobic property and contain a random coil structure.…”

Section: Discussionmentioning

confidence: 84%

“…According to Pata et al [33], blood was collected from crocodiles and transferred to 15 mL sterile tubes that contained 0.5 M EDTA. Later, in order to obtain red blood cells, the blood mixture was stored at 4°C overnight, whereupon leukocytes and plasma were removed.…”

Section: Crocodile Bloodmentioning

confidence: 99%

“…Moreover, they show improvement of wound healing in a mouse model. More recently, Leucrocin I-IV from white blood cell extract of C. siamensis has shown strong antibacterial activity toward Staphylococcus epidermidis, Salmonella typhi and Vibrio cholerae [33]. The antimicrobial action of American alligator Hb shows that both the a-chain and the b-chain can inhibit the growth of Gram-negative bacteria, such as Escherichia coli, Pseudomonas aeruginosa and the fungus Candida albicans [16].…”

Section: Introductionmentioning

confidence: 99%

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Complete Amino Acid Sequence of Globin Chains and Biological Activity of Fragmented Crocodile Hemoglobin (Crocodylus siamensis)

et al. 2012

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Hemoglobin, α-chain, β-chain and fragmented hemoglobin of Crocodylus siamensis demonstrated both antibacterial and antioxidant activities. Antibacterial and antioxidant properties of the hemoglobin did not depend on the heme structure but could result from the compositions of amino acid residues and structures present in their primary structure. Furthermore, thirteen purified active peptides were obtained by RP-HPLC analyses, corresponding to fragments in the α-globin chain and the β-globin chain which are mostly located at the N-terminal and C-terminal parts. These active peptides operate on the bacterial cell membrane. The globin chains of Crocodylus siamensis showed similar amino acids to the sequences of Crocodylus niloticus. The novel amino acid substitutions of α-chain and β-chain are not associated with the heme binding site or the bicarbonate ion binding site, but could be important through their interactions with membranes of bacteria.

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Section: Discussionmentioning

confidence: 84%

Section: Crocodile Bloodmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Complete Amino Acid Sequence of Globin Chains and Biological Activity of Fragmented Crocodile Hemoglobin (Crocodylus siamensis)

et al. 2012

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“…Planar layer chromatography coupled with antibacterial assay (direct bioautography, DB) [4,5] is a screening and biomonitoring tool that is high-throughput, rapid, easy to perform and suitable in such a workflow [6,7]. Compared to HPLC-antibacterial assay [1,2], the benefits of DB are: 1.…”

Section: Introductionmentioning

confidence: 99%

“…Such analyses point out compounds with the desired activity in a complex matrix, irrespectively of their chemical nature and ensure a subsequent highly targeted procedure including characterization, bioactivity assayguided isolation and identification of the components in question [1][2][3]. Planar layer chromatography coupled with antibacterial assay (direct bioautography, DB) [4,5] is a screening and biomonitoring tool that is high-throughput, rapid, easy to perform and suitable in such a workflow [6,7].…”

Section: Introductionmentioning

confidence: 99%

Layer chromatography-bioassays directed screening and identification of antibacterial compounds from Scotch thistle

Móricz

Krüzselyi

Alberti

et al. 2017

Journal of Chromatography A

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Highlights:-First direct transfer of OPLC mobile phase to flash chromatography -Antibacterial profiling of Scotch thistle (Onopordum acanthium L.) leaf extract -TLC/OPLC-DB using plant and human pathogen bacteria and a probiotic, human gut bacterium L. plantarum utilized for investigation of the extract against eight bacterial strains including two plant and three human pathogens and a soil, a marine and a probiotic human gut bacteria. Antibacterial fractions obtaining infusion-transfusion OPLC were transferred to HPLC-MS/MS analysis that resulted in the characterization of three active compounds and two of them were identified as, linoleic and linolenic acid. OPLC method was adopted to preparative-scale flash chromatography for the isolation of the third active compound, which was identified after a further semi-preparative HPLC purification as the germacranolide sesquiterpene lactone onopordopicrin. Pure onopordopicrin exhibited antibacterial activity that was specified as minimal inhibitory concentration in the liquid phase as well.

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Studies of the mechanism of an antibacterial peptide (cecropinA–magainin) on methicillin‐resistant Staphylococcus aureus membranes

Zhu

Liu

et al. 2015

Biotech and App Biochem

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As bacterial resistance becomes increasingly common, a new hybrid peptide, cecropinA-magainin (KWALSKEGPGKFLGKKKKF), has been developed that can kill a broad spectrum of bacteria without damaging human cells. The mechanism of antibacterial toxicity for the hybrid peptides is unknown. Herein, we investigate the localization of the hybrid peptide in methicillin-resistant Staphylococcus aureus (MRSA). The minimum inhibitory concentration was 64 µg/mL. The hybrid peptides could enhance the hydrophobicity of MRSA. Dye leakage experiments showed that the hybrid peptides caused dye leakage from liposomes. The hybrid peptides influenced the permeability of the outer membrane and plasma membrane of MRSA. After cecropinA-magainin treatment of MRSA, the membrane ultrastructure was damaged and the concentration of K increased. Ultimately, the peptide destroyed the integrity of the bacterial cell membrane, allowing the dye propidium iodide to enter the cytoplasm. Therefore, the hybrid antibacterial peptide can kill MRSA.

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Characterization of the novel antibacterial peptide Leucrocin from crocodile (Crocodylus siamensis) white blood cell extracts

Cited by 83 publications

References 41 publications

Complete Amino Acid Sequence of Globin Chains and Biological Activity of Fragmented Crocodile Hemoglobin (Crocodylus siamensis)

Complete Amino Acid Sequence of Globin Chains and Biological Activity of Fragmented Crocodile Hemoglobin (Crocodylus siamensis)

Layer chromatography-bioassays directed screening and identification of antibacterial compounds from Scotch thistle

Studies of the mechanism of an antibacterial peptide (cecropinA–magainin) on methicillin‐resistant Staphylococcus aureus membranes

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