Heparin acts as a structural component of β-endorphin amyloid fibrils rather than a simple aggregation promoter. Nespovitaya, N., Mahou, P., Laine, R., F., Schierle, G., S., K., Kaminski, C., F., Dalayeun, J., F., Nores, J., M., Bergal, S., Maji, S., K., Perrin, M., H., Sawaya, M., R., Jessberger, S., Vadodaria, K., Rissman, R., A., Singru, P., S., Nilsson, K., P., R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R., Nespovitaya, N., Gath, J., Barylyuk, K., Seuring, C., Meier, B., H., Riek, R., Fitzpatrick, A., W., P., Park, S., T., Zewail, A., H., Dong, J., Castro, C., E., Boyce, M., C., Lang, M., J., Lindquist, S., Iannuzzi, C., Irace, G., Sirangelo, I., Hatters, D., M., Minton, A., P., Howlett, G., J., Ma, Q., Fan, J., Zhou, Z., Zhou, B., Meng, S., Hu, J., Chen, J., Liang, Y., Laine, R., F., Schierle, G., S., K., Linde, S., v., d., Kaminski, C., F., Laine, R., F., Albecka, A., Linde, S., v., d., Rees, E., J., Crump, C., M., Kaminski, C., F., Pinotsi, D., Michel, C., H., Buell, A., K., Laine, R., F., Mahou, P., Dobson, C., M., Kaminski, C., F., Schierle, G., S., K., Rabenstein, D., L., Hermann, R., Walther, P., Müller, M., Heilemann, M., Linde, S., v., d., Schuttpelz, M., Kasper, R., Seefeldt, B., Mukherjee, A., Tinnefeld, P., Sauer, M., Hell, S., W., Wichmann, J., Cohlberg, J., A., Li, J., Uversky, V., N., Fink, A., L., Jha, S., Patil, S., M., Gibson, J., Nelson, C., E., Alder, N., N., Alexandrescu, A., T., Valle-Delgado, J., J., Alfonso-Prieto, M., Groot, N., S., d., Ventura, S., Samitier, J., Rovira, C., Fernandez-Busquets, X., Valle-Delgado, J., J., Alfonso-Prieto, M., Groot, N., S., d., Ventura, S., Samitier, J., Rovira, C., Fernàndez-Busquets, X., Madine, J., Davies, H., A., Hughes, E., Middleton, D., A., Calamai, M., Kumita, J., R., Mifsud, J., Parrini, C., Ramazzotti, M., Ramponi, G., Taddei, N., Chiti, F., & Dobson, C., M. Chem. Commun., 47:311-320, Royal Society of Chemistry, 2017.
Heparin acts as a structural component of β-endorphin amyloid fibrils rather than a simple aggregation promoter [pdf]Paper  Heparin acts as a structural component of β-endorphin amyloid fibrils rather than a simple aggregation promoter [link]Website  abstract   bibtex   
The aggregation promoter heparin is commonly used to study the aggregation kinetics and biophysical properties of protein amyloids. However, the underlying mechanism for amyloid promotion by heparin remains poorly understood. In the case of the neuropeptide β-endorphin that can reversibly adopt a functional amyloid form in nature, aggregation in the presence of heparin leads to a loss of function. Applying correlative optical super-resolution microscopy methods, we show that heparin incorporates into emerging β-endorphin fibrils forming an integral component and is essential for amyloid templating. This will have direct implications on β-endorphin's normal physiological function and raises concerns on the biological relevance of heparin-promoted amyloid models.
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 title = {Heparin acts as a structural component of β-endorphin amyloid fibrils rather than a simple aggregation promoter},
 type = {article},
 year = {2017},
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 pages = {311-320},
 volume = {47},
 websites = {http://xlink.rsc.org/?DOI=C6CC09770G},
 publisher = {Royal Society of Chemistry},
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 abstract = {The aggregation promoter heparin is commonly used to study the aggregation kinetics and biophysical properties of protein amyloids. However, the underlying mechanism for amyloid promotion by heparin remains poorly understood. In the case of the neuropeptide β-endorphin that can reversibly adopt a functional amyloid form in nature, aggregation in the presence of heparin leads to a loss of function. Applying correlative optical super-resolution microscopy methods, we show that heparin incorporates into emerging β-endorphin fibrils forming an integral component and is essential for amyloid templating. This will have direct implications on β-endorphin's normal physiological function and raises concerns on the biological relevance of heparin-promoted amyloid models.},
 bibtype = {article},
 author = {Nespovitaya, N. and Mahou, P. and Laine, R. F. and Schierle, G. S. Kaminski and Kaminski, C. F. and Dalayeun, J. F. and Nores, J. M. and Bergal, S. and Maji, S. K. and Perrin, M. H. and Sawaya, M. R. and Jessberger, S. and Vadodaria, K. and Rissman, R. A. and Singru, P. S. and Nilsson, K. P. R. and Simon, R. and Schubert, D. and Eisenberg, D. and Rivier, J. and Sawchenko, P. and Vale, W. and Riek, R. and Nespovitaya, N. and Gath, J. and Barylyuk, K. and Seuring, C. and Meier, B. H. and Riek, R. and Fitzpatrick, A. W. P. and Park, S. T. and Zewail, A. H. and Dong, J. and Castro, C. E. and Boyce, M. C. and Lang, M. J. and Lindquist, S. and Iannuzzi, C. and Irace, G. and Sirangelo, I. and Hatters, D. M. and Minton, A. P. and Howlett, G. J. and Ma, Q. and Fan, J.-B. and Zhou, Z. and Zhou, B.-R. and Meng, S.-R. and Hu, J.-Y. and Chen, J. and Liang, Y. and Laine, R. F. and Schierle, G. S. Kaminski and Linde, S. van de and Kaminski, C. F. and Laine, R. F. and Albecka, A. and Linde, S. van de and Rees, E. J. and Crump, C. M. and Kaminski, C. F. and Pinotsi, D. and Michel, C. H. and Buell, A. K. and Laine, R. F. and Mahou, P. and Dobson, C. M. and Kaminski, C. F. and Schierle, G. S. Kaminski and Rabenstein, D. L. and Hermann, R. and Walther, P. and Müller, M. and Heilemann, M. and Linde, S. van de and Schuttpelz, M. and Kasper, R. and Seefeldt, B. and Mukherjee, A. and Tinnefeld, P. and Sauer, M. and Hell, S. W. and Wichmann, J. and Cohlberg, J. A. and Li, J. and Uversky, V. N. and Fink, A. L. and Jha, S. and Patil, S. M. and Gibson, J. and Nelson, C. E. and Alder, N. N. and Alexandrescu, A. T. and Valle-Delgado, J. Jose and Alfonso-Prieto, M. and Groot, N. S. de and Ventura, S. and Samitier, J. and Rovira, C. and Fernandez-Busquets, X. and Valle-Delgado, J. J. and Alfonso-Prieto, M. and Groot, N. S. de and Ventura, S. and Samitier, J. and Rovira, C. and Fernàndez-Busquets, X. and Madine, J. and Davies, H. A. and Hughes, E. and Middleton, D. A. and Calamai, M. and Kumita, J. R. and Mifsud, J. and Parrini, C. and Ramazzotti, M. and Ramponi, G. and Taddei, N. and Chiti, F. and Dobson, C. M.},
 journal = {Chem. Commun.}
}
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