Protegrins are small peptides containing 16-18 amino acid residues. Protegrins were first discovered in porcine leukocytes and were found to have antimicrobial activity against bacteria, fungi, and some enveloped viruses. The amino acid composition of protegrins contains six positively charged arginine residues and four cysteine residues. Their secondary structure is classified as cysteine-rich β-sheet antimicrobial peptides, AMPs, that display limited sequence similarity to certain defensins and . In solution, the peptides fold to form an anti-parallel β-strand with the structure stabilized by two cysteine bridges formed among the four cysteine residues. Recent studies suggest that protegrins can bind to lipopolysaccharide, a property that may help them to insert into the membranes of gra
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| - Protegrin (en)
- Protegryny (pl)
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| - Protegryny – peptydy antydrobnoustrojowe pochodzące z leukocytów wieprzowych, należące do rodziny katelicydyn. Są to kationowe, bogate w cysteinę białka zbudowane z 16-18 aminokwasów, zawierające dwa wiązania dwusiarczkowe, w roztworze przyjmujące strukturę β. Białkiem o najsilniejszych właściwościach przeciwbakteryjnych jest protegryna-1 (PG-1) hamująca rozwój zakażenia dwoinką Neisseria gonorrhoeae, Chlamydia trachomatis L2 oraz serowarami E i MoPn. Szczegółowe badania budowy i funkcji PG-1 wykazały, że amfipatyczna centralna β-płaszczyzna PG-1 jest niezbędna dla ich działania bakteriobójczego. (pl)
- Protegrins are small peptides containing 16-18 amino acid residues. Protegrins were first discovered in porcine leukocytes and were found to have antimicrobial activity against bacteria, fungi, and some enveloped viruses. The amino acid composition of protegrins contains six positively charged arginine residues and four cysteine residues. Their secondary structure is classified as cysteine-rich β-sheet antimicrobial peptides, AMPs, that display limited sequence similarity to certain defensins and . In solution, the peptides fold to form an anti-parallel β-strand with the structure stabilized by two cysteine bridges formed among the four cysteine residues. Recent studies suggest that protegrins can bind to lipopolysaccharide, a property that may help them to insert into the membranes of gra (en)
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| - Protegrins are small peptides containing 16-18 amino acid residues. Protegrins were first discovered in porcine leukocytes and were found to have antimicrobial activity against bacteria, fungi, and some enveloped viruses. The amino acid composition of protegrins contains six positively charged arginine residues and four cysteine residues. Their secondary structure is classified as cysteine-rich β-sheet antimicrobial peptides, AMPs, that display limited sequence similarity to certain defensins and . In solution, the peptides fold to form an anti-parallel β-strand with the structure stabilized by two cysteine bridges formed among the four cysteine residues. Recent studies suggest that protegrins can bind to lipopolysaccharide, a property that may help them to insert into the membranes of gram-negative bacteria and permeabilize them. (en)
- Protegryny – peptydy antydrobnoustrojowe pochodzące z leukocytów wieprzowych, należące do rodziny katelicydyn. Są to kationowe, bogate w cysteinę białka zbudowane z 16-18 aminokwasów, zawierające dwa wiązania dwusiarczkowe, w roztworze przyjmujące strukturę β. Białkiem o najsilniejszych właściwościach przeciwbakteryjnych jest protegryna-1 (PG-1) hamująca rozwój zakażenia dwoinką Neisseria gonorrhoeae, Chlamydia trachomatis L2 oraz serowarami E i MoPn. Szczegółowe badania budowy i funkcji PG-1 wykazały, że amfipatyczna centralna β-płaszczyzna PG-1 jest niezbędna dla ich działania bakteriobójczego. (pl)
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