scholarly journals Structural and Mechanismic Studies of Lactophoricin Analog, Novel Antibacterial Peptide

2021 ◽  
Vol 22 (7) ◽  
pp. 3734
Author(s):  
Minseon Kim ◽  
Jinyoung Son ◽  
Yongae Kim
Keyword(s):  
Antibacterial Activity ◽  
Bovine Milk ◽  
Pharmacological Action ◽  
Antibacterial Peptide ◽  
Amino Acid Sequences ◽  
Phospholipid Bilayer ◽  
Antibacterial Peptides ◽  
Peptide Analog ◽  
Proteose Peptone ◽  
Peptide Analogs

Naturally derived antibacterial peptides exhibit excellent pharmacological action without the risk of resistance, suggesting a potential role as biologicals. Lactophoricin-I (LPcin-I), found in the proteose peptone component-3 (PP3; lactophorin) of bovine milk, is known to exhibit antibiotic activity against Gram-positive and Gram-negative bacteria. Accordingly, we derived a new antibacterial peptide and investigated its structure–function relationship. This study was initiated by designing antibacterial peptide analogs with better antibacterial activity, less cytotoxicity, and shorter amino acid sequences based on LPcin-I. The structural properties of antibacterial peptide analogs were investigated via spectroscopic analysis, and the antibacterial activity was confirmed by measurement of the minimal inhibitory concentration (MIC). The structure and mechanism of the antibacterial peptide analog in the cell membrane were also studied via solution-state nuclear magnetic resonance (NMR) and solid-state NMR spectroscopy. Through 15N one-dimensional and two-dimensional NMR experiments and 31P NMR experiments, we suggest the 3D morphology and antibacterial mechanism in the phospholipid bilayer of the LPcin analog. This study is expected to establish a system for the development of novel antibacterial peptides and to establish a theoretical basis for research into antibiotic substitutes.

Recent Advances in 1,3,5-Triazine Derivatives as Antibacterial Agents

2020 ◽  
Vol 17 (8) ◽  
pp. 991-1041
Author(s):  
Divya Utreja ◽  
Jagdish Kaur ◽  
Komalpreet Kaur ◽  
Palak Jain
Keyword(s):  
Antibacterial Activity ◽  
Heterocyclic Compounds ◽  
Antibacterial Agents ◽  
Rapid Development ◽  
Pharmacological Action ◽  
Biological Properties ◽  
Vast Array ◽  
Bacterial Diseases ◽  
New Class ◽  
Triazine Derivatives

Triazine, one of the nitrogen containing heterocyclic compounds has attracted the considerable interest of researchers due to the vast array of biological properties such as anti-viral, antitumor, anti-convulsant, analgesic, antioxidant, anti-depressant, herbicidal, insecticidal, fungicidal, antibacterial and anti-inflammatory activities offered by it. Various antibacterial agents have been synthesized by researchers to curb bacterial diseases but due to rapid development in drug resistance, tolerance and side effects, there had always been a need for the synthesis of a new class of antibacterial agents that would exhibit improved pharmacological action. Therefore, this review mainly focuses on the various methods for the synthesis of triazine derivatives and their antibacterial activity.

Proteolysis of caseins and the proteose-peptone fraction of bovine milk

1983 ◽  
Vol 50 (3) ◽  
pp. 275-290 ◽  
Author(s):  
Anthony T. Andrews ◽  
Efstathios Alichanidis
Keyword(s):  
Gel Electrophoresis ◽  
Whey Proteins ◽  
Bovine Milk ◽  
Major Product ◽  
Natural Course ◽  
Pasteurized Milk ◽  
Proteose Peptone ◽  
History Of

SummaryThe proteolysis of highly purified samples of αs1-, αs2-, β-and κ-caseins by porcine plasmin and by bovine plasminogen with urokinase has been examined principally by gel electrophoresis. The resulting peptide band patterns were compared with those of total proteose-peptone (TPP) samples prepared from fresh and stored raw and pasteurized milk, and also with those obtained during the natural course of proteolysis by indigenous enzymes in milk during storage. TPP was found to contain at least 38 components detectable by a single electrophoresis run. Apart from residual traces of whey proteins and intact caseins nearly all of these components were fragments of caseins produced by indigenous plasmin, with products from the breakdown of αs1- and β-casein predominating. Over 90 % of TPP has been accounted for in this way. A fragment consisting of residues 29–105 of β-casein was isolated and characterized from both stored milk and from plasmin digests of β-casein. This fragment was a relatively major product of the natural proteolysis occurring during storage of milk, but contrary to a report in the literature it was not the same as proteose-peptone component 8-slow. Since many of the components of TPP resulted from proteolysis, the composition of TPP was found to vary according to the time and temperature of storage of the milk from which it was prepared. Thus, while the proteose-peptone fraction of milk can easily be defined operationally it cannot be rigorously defined in terms of its composition unless the history of the milk is also defined.

scholarly journals Complete sequences of epidermin and nukacin encoding plasmids from oral-derived Staphylococcus epidermidis and their antibacterial activity

2021 ◽  
Author(s):  
Kenta Nakazono ◽  
Mi Nguyen-Tra Le ◽  
Miki Kawada-Matsuo ◽  
Noy Kimheang ◽  
Junzo Hisatsune ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Amino Acid ◽  
Staphylococcus Epidermidis ◽  
Activity Patterns ◽  
Bacterial Flora ◽  
Complete Sequence ◽  
Oral Bacteria ◽  
Amino Acid Sequences ◽  
Commensal Bacterium ◽  
Complete Sequences

AbstractStaphylococcus epidermidis is a commensal bacterium in humans. To persist in the bacterial flora of the host, some bacteria produce antibacterial factors such as the antimicrobial peptides known as bacteriocins. In this study, we tried to isolate bacteriocin-producing S. epidermidis strains. Among 150 S. epidermidis isolates from the oral cavities of 287 volunteers, we detected two bacteriocin-producing strains, KSE56 and KSE650. Complete genome sequences of the two strains confirmed that they carried the epidermin-harbouring plasmid pEpi56 and the nukacin IVK45-like- harbouring plasmid pNuk650. The amino acid sequence of epidermin from KSE56 was identical to the previously reported sequence, but the epidermin synthesis-related genes were partially different. The prepeptide amino acid sequences of nukacin KSE650 and nukacin IVK45 showed one mismatch, but both mature peptides were entirely similar. pNuk650 was larger and had an additional seven ORFs compared to pIVK45. We then investigated the antibacterial activity of the two strains against several skin and oral bacteria and found their different activity patterns. In conclusion, we report the complete sequences of 2 plasmids coding for bacteriocins from S. epidermidis, which were partially different from those previously reported. Furthermore, this is the first report to show the complete sequence of an epidermin-carrying plasmid, pEpi56.

Self-Assembly of Virulent Amyloid-Derived Peptides into Nanoantibacterials

Nanoscale ◽  
2021 ◽  
Author(s):  
Wenlu Tu ◽  
Ke Xue ◽  
Shaofeng Lou ◽  
Chunlei Zhu ◽  
Zhilin Yu
Keyword(s):  
Antibacterial Activity ◽  
Self Assembly ◽  
Antibacterial Peptides

Current strategies for design of antibacterial peptides show limitation in development of assembled antibacterial peptides due to the challenges in simultaneously balancing the antibacterial activity and assembling behavior. Herein, we...

The formation and structure of some proteose-peptone components

1979 ◽  
Vol 46 (2) ◽  
pp. 215-218 ◽  
Author(s):  
Anthony T. Andrews
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Bovine Milk ◽  
Raw Milk ◽  
Terminal Part ◽  
Proteose Peptone ◽  
Proteolytic Cleavages

SUMMARYTwo constituents of the proteose-peptone fraction of bovine milk have been isolated and characterized. Component 5 (PP5) has been shown to represent residues 1–105 and 1–107 of the β-casein amino acid sequence, while component 8-fast (PP8F) corresponds to residues 1–28 of β-casein. Thus, these proteose-peptones represent the N-terminal portions of the β-casein molecule, produced by proteolytic cleavages which form the γ1-, γ2- and γ3-caseins from the C-terminal part. The continuing formation of the total proteose-peptone fraction, PP5, PP8F and the γ-caseins during storage of raw milk at 18 or 37 °C has also been demonstrated

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