T. P. Knowles and M. J. Buehler, Nanomechanics of functional and pathological amyloid materials, Nat. Nanotechnol, vol.6, pp.469-479, 2011.

D. J. Selkoe, Alzheimer's disease: genes, proteins, and therapy, Physiol. Rev, vol.81, pp.741-766, 2001.

C. M. Dobson, Protein folding and misfolding, Nature, vol.426, pp.884-890, 2003.

D. J. Selkoe, Folding proteins in fatal ways, Nature, vol.426, pp.900-904, 2003.

F. Chiti and C. M. Dobson, Protein misfolding, functional amyloid and human disease, Annu. Rev. Biochem, vol.75, pp.333-366, 2006.

L. Kreplak and U. Aebi, From the polymorphism of amyloid fibrils to their assembly mechanism and cytotoxicity, Adv. Protein Chem, vol.73, pp.217-233, 2006.

C. A. Hauser, S. Maurer-stroh, and I. C. Martins, Amyloid-based nanosensors and nanodevices, Chem. Soc. Rev, vol.43, pp.5326-5345, 2014.

J. Adamcik and R. Mezzenga, Fibrils from a polymer physics perspective, Macromolecules, vol.45, pp.1137-1150, 2012.

C. Li and R. Mezzenga, The interplay between carbon nanomaterials and amyloid fibrils in bio-nanotechnology, Nanoscale, vol.5, pp.6207-6218, 2013.

S. Mankar, A. Anoop, S. Sen, and S. K. Maji, Nanomaterials: amyloids reflect their brighter side, Nano Rev, vol.2, pp.6032-6043, 2011.

I. Cherny and E. Gazit, Amyloids: not only pathological agents but also ordered nanomaterials, Angew. Chem. Int. Ed, vol.47, pp.4062-4069, 2008.

G. Jones, O. Mezzenga, and R. , Inhibiting, promoting, and preserving stability of functional protein fibrils, Soft Matter, vol.8, pp.876-895, 2012.

A. T. Petkova, A structural model for Alzheimer's b-amyloid fibrils based on experimental constraints from solid state NMR, Proc. Natl Acad. Sci. USA, vol.99, pp.16742-16747, 2002.

P. Metrangolo and G. Resnati, Halogen versus hydrogen, Science, vol.321, pp.918-919, 2008.

D. M. Ryan, S. B. Anderson, F. T. Senguen, R. E. Youngman, and B. L. Nilsson, Self-assembly and hydrogelation promoted by F5-phenylalanine, Soft Matter, vol.6, pp.475-479, 2010.

Y. Wang, Z. Zhang, L. Xu, X. Li, and H. Chen, Hydrogels of halogenated Fmoc-short peptides for potential application in tissue engineering, Colloids Surf. B Biointerfaces, vol.104, pp.163-168, 2013.

M. Reches and E. Gazit, Designed aromatic homo-dipeptides: formation of ordered nanostructures and potential nanotechnological applications, Phys. Biol, vol.3, pp.10-19, 2006.

P. Metrangolo, T. Pilati, and G. Resnati, Halogen bonding and other noncovalent interactions involving halogens: a terminology issue, Cryst. Eng. Comm, vol.8, pp.946-947, 2006.

D. M. Ryan, T. M. Doran, S. B. Anderson, and B. L. Nilsson, Effect of C-terminal modification on the self-assembly and hydrogelation of fluorinated Fmoc-Phe derivatives, Langmuir, vol.27, pp.4029-4039, 2011.

D. M. Ryan, S. B. Anderson, and B. L. Nilsson, The influence of side-chain halogenation on the self-assembly and hydrogelation of Fmoc-phenylalanine derivatives, Soft Matter, vol.6, pp.3220-3231, 2010.

G. R. Desiraju, Definition of the halogen bond (IUPAC Recommendations, Pure Appl. Chem, vol.85, pp.1711-1713, 2013.

P. Metrangolo and G. Resnati, Tracing iodine, Nat. Chem, vol.3, p.260, 2011.

P. Metrangolo and G. Resnati, Type II halogen Á Á Á halogen contacts are halogen bonds, IUCrJ, vol.1, pp.5-7, 2014.

G. Berger, N. Berger, M. H. Guillaud, J. Trouillas, and J. L. Vauzelle, Calcitonin-like immunoreactivity of amyloid fibrils in medullary thyroid carcinomas. An immunoelectron microscope study, Virchows Arch. A Pathol. Anat. Histopathol, vol.412, pp.543-551, 1988.

T. Arvinte, A. Cudd, and A. F. Drake, The structure and mechanism of formation of human calcitonin fibrils, J. Biol. Chem, vol.268, pp.6415-6422, 1993.

J. W. Steed, Supramolecular gel chemistry: developments over the last decade, Chem. Commun, vol.47, pp.1379-1383, 2011.

L. Meazza, Halogen-bonding-triggered supramolecular gel formation, Nat. Chem, vol.5, pp.42-47, 2013.

A. Lakshmanana, Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis, Proc. Natl Acad. Sci. USA, vol.110, pp.519-524, 2013.

A. Shtainfeld, T. Sheynis, and R. Jelinek, Specific mutations alter fibrillation kinetics, fiber morphologies, and membrane interactions of pentapeptides derived from human calcitonin, Biochemistry, vol.49, pp.5299-5307, 2010.

C. A. Hauser, Natural tri-to hexapeptides self-assemble in water to amyloid b-type fiber aggregates by unexpected a-helical intermediate structures, Proc. Natl Acad. Sci. USA, vol.108, pp.1361-1366, 2011.

A. Mishra, Ultrasmall natural peptides self-assemble to strong temperature-resistant helical fibers in scaffolds suitable for tissue engineering, Nano Today, vol.6, pp.232-239, 2011.

D. K. Smith, Supramolecular Chemistry: From Molecules to Nanomaterials, 1999.

J. Adamcik, Understanding amyloid aggregation by statistical analysis of atomic force microscopy images, Nat. Nanotechnol, vol.5, pp.423-428, 2010.

M. R. Nilsson, Techniques to study amyloid fibril formation in vitro, Methods, vol.34, pp.151-160, 2004.

B. Shivu, Distinct b-sheet structure in protein aggregates determined by ATR-FTIR spectroscopy, Biochemistry, vol.52, pp.5176-5183, 2013.

V. Vasylyeva, Orthogonal halogen and hydrogen bonds involving a peptide bond model, Cryst. Eng. Comm, vol.16, pp.8102-8105, 2014.
DOI : 10.1039/c4ce01514b

URL : https://pubs.rsc.org/en/content/articlepdf/2014/ce/c4ce01514b

M. T. Messina, Infrared and Raman analyses of the halogen-bonded non-covalent adducts formed by a-$-diiodoperfluoroalkanes with DABCO and other electron donors, J. Mol. Struct, vol.524, pp.87-94, 2000.

V. D. Vliet, Myeloperoxidase and protein oxidation in cystic fibrosis, Am. J. Physiol. Lung Cell. Mol. Physiol, vol.279, pp.537-546, 2000.

S. L. Hazen, 3-chlorotyrosine, a specific marker of myeloperoxidase? Catalyzed oxidation is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima, J. Clin. Invest, vol.99, pp.2075-2075, 1997.

J. P. Gaut, Neutrophils employ the myeloperoxidase system to generate antimicrobial brominating and chlorinating oxidants during sepsis, Proc. Natl Acad. Sci. USA, vol.98, pp.11961-11961, 2001.
DOI : 10.1073/pnas.211190298

W. Wu, Eosinophils generate brominating oxidants in allergen-induced asthma, J. Clin. Invest, vol.105, pp.1455-1463, 2000.
DOI : 10.1172/jci9702

URL : http://www.jci.org/articles/view/9702/files/pdf

J. R. Mazzulli, R. Hodara, S. Lind, and H. Ischiropoulos, Oxidative stress and protein deposition diseases in protein misfolding, aggregation, and conformational diseases, Prot. Rev, vol.4, pp.123-133, 2006.

D. M. Ryan, T. M. Doran, and B. L. Nilsson, Complementary p-p interactions induce multicomponent coassembly into functional fibrils, Langmuir, vol.27, pp.11145-11156, 2011.
DOI : 10.1021/la202070d

E. Gazit, Searching sequence space, Nat. Chem, vol.7, pp.14-15, 2015.

P. W. Frederix, Exploring the sequence space for (tri-)peptide selfassembly to design and discover new hydrogels, Nat. Chem, vol.7, pp.30-37, 2015.
DOI : 10.1038/nchem.2122

G. M. Sheldrick, A short history of SHELX, Acta Crystallogr. Sect. A, vol.64, pp.112-122, 2008.

C. F. Macrae, Mercury CSD 2.0 -new features for the visualization and investigation of crystal structures, J. Appl. Cryst, vol.41, pp.466-470, 2008.

P. Engelhardt, Electron tomography of chromosome structure, Encyclopedia of analytical chemistry, 2006.
DOI : 10.1002/9780470027318.a1405

S. Sirimulla, J. B. Bailey, R. Vegesna, and M. Narayan, Halogen interactions in protein-ligand complexes: implications of halogen bonding for rational drug design, J. Chem. Inf. Model, vol.53, pp.2781-2791, 2013.

Y. Lu, Triangular halogen trimers. A DFT study of the structure, cooperativity, and vibrational properties, J. Phys. Chem. A, vol.109, pp.11956-11961, 2005.