**7. Conclusions**

Amyloid formation and related disorders present examples of situations where there is fundamental dependence on protein structure, its variation(s), abundance, and the consequences of alternative conformation(s). Because the molecules involved are quite different for each type of amyloid disease, different organs may be involved, and stabilizing or eliminating the precursors likely will vary. Successful therapeutic intervention will likely be unique to each type of amyloidosis. The basic concerns are similar, however, and considerable progress has already clarified both the problem(s) and the options.

## **Acknowledgements**

Support for these studies was provided by generous gifts to the author from Stuart Bainum, Mary Nell and George A. Berry, Ethelbert Cooper, Gloria and Edward Felsenthal, Ruth Frey, Shirley Griffin, Ruth and George Harms, Yancey and David Hillegas, Diantha Johnson, Bassem Kudsi, Steven Lazinsky, Judy Lewent and Mark Shapiro, Terrence O'Donnell, Jay Ripley, Israel Vainboim, the Foundation for Greater Good, the Health Network Foundation, and the MetLife Foundation.

**185**

**Author details**

George H. Sack Jr.

provided the original work is properly cited.

School of Medicine, Baltimore, Maryland, USA

\*Address all correspondence to: gsack@jhmi.edu

*Pathophysiology of Amyloid Fibril Formation DOI: http://dx.doi.org/10.5772/intechopen.81965*

© 2019 The Author(s). Licensee IntechOpen. This chapter is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/ by/3.0), which permits unrestricted use, distribution, and reproduction in any medium,

Departments of Biological Chemistry and Medicine, Johns Hopkins University
