F. Chiti, C. M. Dobson, F. Misfolding, . Amyloid, I. W. And-human-disease-hamley et al., The Amyloid Beta Peptide: A Chemist's Perspective Role in Alzheimer's and Fibrillization Dependence of ?-Synuclein Aggregate Morphology on Solution Conditions Functional Amyloidogenesis and Cytotoxicity?Insights into Biology and Pathology, Amyloids Protect the Silkmoth Oocyte and Embryo, pp.333-366, 2000.

M. A. Horton, C. M. Dobson, C. E. Macphee, B. Watt, G. Van-niel et al., Functionalised Amyloid Fibrils for Roles in Cell Adhesion PMEL: A Pigment Cell-Specific Model for Functional Amyloid Formation (9) Otzen, D. Functional Amyloid: Turning Swords into Plowshares, Biomaterials Pigment Cell Melanoma Res. Prion, vol.29, issue.4410, pp.1553-1562, 2008.

S. P. Jarvis, M. C. Garcia-sherman, and T. Lundberg, Nanoscale Mechanical Characterisation of Amyloid Fibrils Discovered in a Natural Adhesive, J. Biol . Phys, vol.32, issue.511, pp.393-401, 2007.

P. N. Lipke, S. A. Klotz, D. M. Fowler, A. V. Koulov, W. E. Balch et al., Functional Amyloid ? from Bacteria to Humans Functional Amyloids in Bacteria Functional Amyloid Formation within Mammalian Tissue On Functional Amyloids of Muscle Proteins of Titin Family Functional Amyloids As Natural Storage of Peptide Hormones in Pituitary Secretory Granules Organization: Octapeptide Self-Assembly into Nanotubes of Viral Capsid-like Dimension, Biofilm in Human Deep Mycoses: Fungal Amyloid Is Bound by Host Serum Amyloid P Component. NPJ Biofilms Microbiomes 2015 e6. (15) Podlubnaya Proc. Natl. Acad. Sci18) Valéry, C.; Artzner, F.; Paternostre, M. Peptide Nanotubes: Molecular Organisations, Self-Assembly Mechanisms and Applications Kasotakis, E.; et al. Atomic View of the Histidine Environment Stabilizing Higher-pH Conformations of pH-Dependent Proteins, pp.217-224, 1920.

F. Besselievre, Control of Peptide Nanotube Diameter by Chemical Modifications of an Aromatic Residue Involved in a Single Close Contact Peptide Hormones and Lipopeptides: From Self-Assembly to Therapeutic Applications: Peptides: From Self-Assembly to Therapeutic Applications Peptide Based Self- Assembled Nanostructures: Implications in Drug Delivery and Tissue Engineering, Proc. Natl. Acad. Sci 2017. (22) Panda Burkhard, P. Nanoscale Assemblies and Their Biomedical Applications, pp.7679-7684, 2011.

J. R. Soc, Y. Nagai, L. D. Unsworth, S. Koutsopoulos, S. Zhang et al., Slow Release of Molecules in Self-Assembling Peptide Nanofiber Scaffold, J. Controlled Release, vol.1025, issue.1151, pp.20120740-20120740, 2006.

J. A. Cordero and C. Peraire, Development of Peptide 3D Structure Mimetics: Rational Design of Novel Peptoid Cholecystokinin Receptor Antagonists Neural Regulation of Pancreatic Hormone Secretion by the C-Terminal Tetrapeptide of CCK (29) Rehfeld, J. F. Immunochemical Studies on Cholecystokinin . II. Distribution and Molecular Heterogeneity in the Central Nervou Ssystem and Small Intestine of Man and Hog Characterization of Preprocholecystokini Products in the Porcine Cerebral Cortex - Evidence of Different Processing Pathways Cholecystokinin Receptors in the Brain: Characterization and Distribution The Physiology of Learning and Memory: Role of Peptides and Stress (33) Larsson, L.-I.; Jens F. Rehfeld. A Peptide Resembling COOH-Terminal Tetrapeptide Amide of Gastrin from a New Gastrointestinal Endocrine Cell Type The Life Cycle of the Gastrin Granule Reversible Chemoselective Tagging and Functionalization of Methionine Containing Peptides Preparation of Multifunctional and Multireactive Polypeptide via Methionine Alkylation (37) Boultif, A.; Louër, D. Powder Pattern Indexing with the Dichotomy Method Alzheimer's Amyloid Fibrils; Structure and Assembly, Autogel: A New Lanreotide Prolonged Release Formulation. Proc Int Symp Control Rel Bio Mat40) Krimm, S.; Bandekar, J. Vibrational Spectroscopy and Conformation of Peptides, Polypeptides, and Proteins42) Byler, D. M.; Susi, H. Examination of the Secondary Structure of Proteins by Deconvolved FTIR Spectra43) Zandomeneghi, G.; Krebs, M. R. H.; McCammon, M. G.; Fändrich, M. FTIR Reveals Structural Differences between Native ?-Sheet Proteins and Amyloid Fibrils. Protein Sci, pp.798-799, 1978.

V. Raussens, T. Atr-ftir-miyazawa, E. Blout, and S. Lecomte, Tool to Investigate Amyloid Proteins (45) Barth, A. The Infrared Absorption of Amino Acid Side Chains The Infrared Spectra of Polypeptides in Various Conformations: Amide I and II bands1, Biochim. Biophys. Acta BBA - Biomembr. Prog. Biophys. Mol. Biol. J. Am. Chem. Soc, vol.2013, issue.833, pp.1828-2328, 1961.

J. Manero, R. Cherif-cheikh, M. Paternostre, C. Valéry, T. Miura et al., Tryptophan Raman Bands Sensitive to Hydrogen Bonding and Side-Chain Conformation Mechanisms of Tryptophan Fluorescence Shifts in Proteins (51) Lakowicz Multiple Quantum Solid-State NMR Indicates a Parallel, Not Antiparallel, Organization of ?-Sheets in Alzheimer's ?-Amyloid Fibrils Supramolecular Structure in Full-Lenght Alzheimer's Fibrils: Evidence for a Parallel ?-Sheet Organization from Solid- State Nuclear Magnetic Resonance Prediction of Sequence-Dependent and Mutational Effects on the Aggregation of Peptides and Proteins Insight into the Structure of Amyloid Fibrils from the Analysis of Globular Proteins: A Server for the Prediction and Evaluation Of " hot Spots " of Aggregation in Polypeptides Prediction of Aggregation-Prone Regions in Structured Proteins Electron Microscopic Appearances and Implications of Neuropeptide Fibrillary Forms Segmental Polymorphism in a Functional Amyloid Dynamic Assembly and Disassembly of Functional ?-Endorphin Amyloid Fibrils, Lamination and Spherulite-like Compaction of a Hormone's Native Amyloid-like Nanofibrils: Spectroscopic Insights into Key Interactions. Faraday Discuss. 2013. (48) Takeuchi, H. Raman Structural Markers of Tryptophan and Histidine Side Chains in Proteins Proc. Natl. Acad. Sci Eisenberg, D. Identifying the Amylome, Proteins Capable of Forming Amyloid-like Fibrils. Proc. Natl. Acad. Sci62) Kurouski, D.; Lauro, W.; Lednev, I. K. Amyloid Fibrils Are " alive " : Spontaneous Refolding from One Polymorph to Another Cherif-Cheikh, R.; Paternostre, M. Self-Association of a Peptide in Solution: From ?-Sheet Filaments to Large Embedded Nanotubes, pp.305-317, 1981.

. C. Am, F. Gobeaux, N. Fay, C. Tarabout, C. Mériadec et al., Structural Role of Counterions Adsorbed on Self-Assembled Peptide Nanotubes Effects of pH and Charge State on Peptide Assembly: The YVIFL Model System Novo Designed Peptide-Based Amyloid Fibrils, Proc. Natl. Acad. Sci68) Dannies, P. S. Prolactin and Growth Hormone Aggregates in Secretory Granules: The Need to Understand the Structure of the Aggregate, pp.846-856, 2002.

M. Henze, S. T. Kumar, M. Fändrich, H. A. Scheidt, D. Huster et al., Structural Characterization of Amyloid Fibrils from the Human Parathyroid Hormone, 70) Grondelle, W. van; Iglesias, C. L.; Coll, pp.249-257

M. Paternostre, F. Lacombe, M. Cardus, G. Martinez, M. Montes et al., Spontaneous Fibrillation of the Native Neuropeptide Hormone Somatosta- tin-14 Neuropeptides: Regulators of Physiological Processes Related Fragments and Analogs by Human and Rat Plasma in Vitro The Role of Assembly in Insulin's Biosynthesis, J. Struct. Biol. Koulitscher, D.; Moroder, L.; Deschodt-Lanckman, M. Degradation of Cholecytokinin Octopeptide Regul. Pept. Curr. Opin. Struct. Biol, vol.160, issue.8, pp.211-223, 1982.

E. Waelkens, F. Chimienti, and G. A. Rutter, Insulin Crystallization Depends on Zinc Transporter ZnT8 Expression , but Is Not Required for Normal Glucose Homeostasis in Mice Insulin Microcrystal Suspension as a Long-Acting Formulation for Pulmonary Delivery (77) Minton, A. P. Implications of Macromolecular Crowding for Protein Assembly, Proc. Natl. Acad. Sci79) Arvan, P.; Castle, D. Sorting and Storage during Secretory Granule Biogenesis: Looking Backward and Looking Forward, pp.14872-14877, 1987.