Sandbox Reserved 1099: Difference between revisions

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In mammalian skin two classes of peptides with antibacterial function are present such as cathelicidins<ref> Gallo, R.L., Ono, M., Povsic, T., Page, C., Eriksson, E., Klagsbrun, M., Bernfield, M., 1994. Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds. Proceedings of the National Academy of Sciences 91, 11035–11039. https://doi.org/10.1073/pnas.91.23.11035 </ref> and β-defensins.<ref> Harder, J., Bartels, J., Christophers, E., Schröder, J.-M., 1997. A peptide antibiotic from human skin. Nature 387, 861–861. https://doi.org/10.1038/43088</ref> Dermcidin forms another category of antimicrobial peptides expressed in human eccrine sweat glands. The dark mucous cells of the sweat glands produce DCD which is then found in the golgi complex and in secretory granules. After proteolytic processes, a form of 47 amino acids (DCD-1) of the original C-terminus is present in the sweat around 1-10 µg/ml. Spread by the sweat over the skin, DCD-1 acts like a regulator of the skin flora. The antimicrobial activity of DCD-1 is not only stable under different pH and salt conditions of the media but also under sweat-similar conditions.<ref> Schittek, B., Hipfel, R., Sauer, B., Bauer, J., Kalbacher, H., Stevanovic, S., Schirle, M., Schroeder, K., Blin, N., Meier, F., Rassner, G., Garbe, C., 2001. Dermcidin: a novel human antibiotic peptide secreted by sweat glands. Nat Immunol 2, 1133–1137. https://doi.org/10.1038/ni732 </ref>
In mammalian skin two classes of peptides with antibacterial function are present such as cathelicidins<ref> Gallo, R.L., Ono, M., Povsic, T., Page, C., Eriksson, E., Klagsbrun, M., Bernfield, M., 1994. Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds. Proceedings of the National Academy of Sciences 91, 11035–11039. https://doi.org/10.1073/pnas.91.23.11035 </ref> and β-defensins.<ref> Harder, J., Bartels, J., Christophers, E., Schröder, J.-M., 1997. A peptide antibiotic from human skin. Nature 387, 861–861. https://doi.org/10.1038/43088</ref> Dermcidin forms another category of antimicrobial peptides expressed in human eccrine sweat glands. The dark mucous cells of the sweat glands produce DCD which is then found in the golgi complex and in secretory granules. After proteolytic processes, a form of 47 amino acids (DCD-1) of the original C-terminus is present in the sweat around 1-10 µg/ml. Spread by the sweat over the skin, DCD-1 acts like a regulator of the skin flora. The antimicrobial activity of DCD-1 is not only stable under different pH and salt conditions of the media but also under sweat-similar conditions.<ref> Schittek, B., Hipfel, R., Sauer, B., Bauer, J., Kalbacher, H., Stevanovic, S., Schirle, M., Schroeder, K., Blin, N., Meier, F., Rassner, G., Garbe, C., 2001. Dermcidin: a novel human antibiotic peptide secreted by sweat glands. Nat Immunol 2, 1133–1137. https://doi.org/10.1038/ni732 </ref>


The overall negatively charged DCD-1L is a one amino acid longer DCD-1 and shows beside the antimicrobial activity against ''Escherichia coli'', ''Staphylococcus aureus'' and ''Enterococcus faecalis'' additional high fungicidal activity on ''Candida albicans''.<ref> Schittek, B., Hipfel, R., Sauer, B., Bauer, J., Kalbacher, H., Stevanovic, S., Schirle, M., Schroeder, K., Blin, N., Meier, F., Rassner, G., Garbe, C., 2001. Dermcidin: a novel human antibiotic peptide secreted by sweat glands. Nat Immunol 2, 1133–1137. https://doi.org/10.1038/ni732 </ref> The first three amino acids (SSL) up to the 23th amino acids of DCD-1L is a region which appears to be responsible for the antibacterial activity. The killing of bacteria rises significantly after 2 – 3 hours of incubation which is not driven by a permeabilization of the outer nor inner bacterial membrane.<ref> Steffen, H., Rieg, S., Wiedemann, I., Kalbacher, H., Deeg, M., Sahl, H.-G., Peschel, A., Gotz, F., Garbe, C., Schittek, B., 2006. Naturally Processed Dermcidin-Derived Peptides Do Not Permeabilize Bacterial Membranes and Kill Microorganisms Irrespective of Their Charge. Antimicrobial Agents and Chemotherapy 50, 2608–2620. https://doi.org/10.1128/AAC.00181-06 </ref> However, some authors are not in agreement on this with each other<ref> Song, C., Weichbrodt, C., Salnikov, E.S., Dynowski, M., Forsberg, B.O., Bechinger, B., Steinem, C., de Groot, B.L., Zachariae, U., Zeth, K., 2013. Crystal structure and functional mechanism of a human antimicrobial membrane channel. Proceedings of the National Academy of Sciences 110, 4586–4591. https://doi.org/10.1073/pnas.1214739110 </ref> since it was also detected that DCD-1L creates ion channels into the bacterial membranes promoted by Zn<sup>2+</sup>.<ref> Paulmann, M., Arnold, T., Linke, D., Özdirekcan, S., Kopp, A., Gutsmann, T., Kalbacher, H., Wanke, I., Schuenemann, V.J., Habeck, M., Bürck, J., Ulrich, A.S., Schittek, B., 2012. Structure-Activity Analysis of the Dermcidin-derived Peptide DCD-1L, an Anionic Antimicrobial Peptide Present in Human Sweat. J. Biol. Chem. 287, 8434–8443. https://doi.org/10.1074/jbc.M111.332270 </ref>
The overall negatively charged DCD-1L is a one amino acid longer DCD-1 and shows beside the antimicrobial activity against [https://en.wikipedia.org/wiki/Escherichia_coli_ ''Escherichia coli''], [https://en.wikipedia.org/wiki/Staphylococcus_aureus_ ''Staphylococcus aureus''] and [https://en.wikipedia.org/wiki/Enterococcus_faecalis_ ''Enterococcus faecalis''] additional high fungicidal activity on [https://en.wikipedia.org/wiki/Candida_albicans_ ''Candida albicans''].<ref> Schittek, B., Hipfel, R., Sauer, B., Bauer, J., Kalbacher, H., Stevanovic, S., Schirle, M., Schroeder, K., Blin, N., Meier, F., Rassner, G., Garbe, C., 2001. Dermcidin: a novel human antibiotic peptide secreted by sweat glands. Nat Immunol 2, 1133–1137. https://doi.org/10.1038/ni732 </ref> The first three amino acids (SSL) up to the 23th amino acids of DCD-1L is a region which appears to be responsible for the antibacterial activity. The killing of bacteria rises significantly after 2 – 3 hours of incubation which is not driven by a permeabilization of the outer nor inner bacterial membrane.<ref> Steffen, H., Rieg, S., Wiedemann, I., Kalbacher, H., Deeg, M., Sahl, H.-G., Peschel, A., Gotz, F., Garbe, C., Schittek, B., 2006. Naturally Processed Dermcidin-Derived Peptides Do Not Permeabilize Bacterial Membranes and Kill Microorganisms Irrespective of Their Charge. Antimicrobial Agents and Chemotherapy 50, 2608–2620. https://doi.org/10.1128/AAC.00181-06 </ref> However, some authors are not in agreement on this with each other<ref> Song, C., Weichbrodt, C., Salnikov, E.S., Dynowski, M., Forsberg, B.O., Bechinger, B., Steinem, C., de Groot, B.L., Zachariae, U., Zeth, K., 2013. Crystal structure and functional mechanism of a human antimicrobial membrane channel. Proceedings of the National Academy of Sciences 110, 4586–4591. https://doi.org/10.1073/pnas.1214739110 </ref> since it was also detected that DCD-1L creates ion channels into the bacterial membranes promoted by Zn<sup>2+</sup>.<ref> Paulmann, M., Arnold, T., Linke, D., Özdirekcan, S., Kopp, A., Gutsmann, T., Kalbacher, H., Wanke, I., Schuenemann, V.J., Habeck, M., Bürck, J., Ulrich, A.S., Schittek, B., 2012. Structure-Activity Analysis of the Dermcidin-derived Peptide DCD-1L, an Anionic Antimicrobial Peptide Present in Human Sweat. J. Biol. Chem. 287, 8434–8443. https://doi.org/10.1074/jbc.M111.332270 </ref>


derived peptides described before modulate immune response (against particular micro-organism)
derived peptides described before modulate immune response (against particular micro-organism)
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