메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

Supramolecular amplification of amyloid self-assembly by iodination

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; AROMATIC AMINO ACID; CALCITONIN; HALOGEN; HYDROGEN; IODINE; PENTAPEPTIDE; PHENYLALANINE;

EID: 84934784495     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms8574     Document Type: Article
Times cited : (83)

References (50)
  • 1
    • 79961211353 scopus 로고    scopus 로고
    • Nanomechanics of functional and pathological amyloid materials
    • Knowles, T. P. J. & Buehler, M. J. Nanomechanics of functional and pathological amyloid materials. Nat. Nanotechnol. 6, 469-479 (2011).
    • (2011) Nat. Nanotechnol. , vol.6 , pp. 469-479
    • Knowles, T.P.J.1    Buehler, M.J.2
  • 2
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe, D. J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81, 741-766 (2001).
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 3
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. Protein folding and misfolding. Nature 426, 884-890 (2003).
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 4
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe, D. J. Folding proteins in fatal ways. Nature 426, 900-904 (2003).
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 5
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid and human disease
    • Chiti, F. & Dobson, C. M. Protein misfolding, functional amyloid and human disease. Annu. Rev. Biochem. 75, 333-366 (2006).
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 6
    • 33845637320 scopus 로고    scopus 로고
    • From the polymorphism of amyloid fibrils to their assembly mechanism and cytotoxicity
    • Kreplak, L. & Aebi, U. From the polymorphism of amyloid fibrils to their assembly mechanism and cytotoxicity. Adv. Protein Chem. 73, 217-233 (2006).
    • (2006) Adv. Protein Chem. , vol.73 , pp. 217-233
    • Kreplak, L.1    Aebi, U.2
  • 8
    • 84856873460 scopus 로고    scopus 로고
    • Fibrils from a polymer physics perspective
    • Adamcik, J. & Mezzenga, R. Fibrils from a polymer physics perspective. Macromolecules 45, 1137-1150 (2012).
    • (2012) Macromolecules , vol.45 , pp. 1137-1150
    • Adamcik, J.1    Mezzenga, R.2
  • 9
    • 84879870006 scopus 로고    scopus 로고
    • The interplay between carbon nanomaterials and amyloid fibrils in bio-nanotechnology
    • Li, C. & Mezzenga, R. The interplay between carbon nanomaterials and amyloid fibrils in bio-nanotechnology. Nanoscale 5, 6207-6218 (2013).
    • (2013) Nanoscale , vol.5 , pp. 6207-6218
    • Li, C.1    Mezzenga, R.2
  • 10
    • 84860315046 scopus 로고    scopus 로고
    • Nanomaterials: Amyloids reflect their brighter side
    • Mankar, S., Anoop, A., Sen, S. & Maji, S. K. Nanomaterials: amyloids reflect their brighter side. Nano Rev. 2, 6032-6043 (2011).
    • (2011) Nano Rev. , vol.2 , pp. 6032-6043
    • Mankar, S.1    Anoop, A.2    Sen, S.3    Maji, S.K.4
  • 11
    • 47049100201 scopus 로고    scopus 로고
    • Amyloids: Not only pathological agents but also ordered nanomaterials
    • Cherny, I. & Gazit, E. Amyloids: not only pathological agents but also ordered nanomaterials. Angew. Chem. Int. Ed. 47, 4062-4069 (2008).
    • (2008) Angew. Chem. Int. Ed. , vol.47 , pp. 4062-4069
    • Cherny, I.1    Gazit, E.2
  • 12
    • 84855445083 scopus 로고    scopus 로고
    • Inhibiting, promoting, and preserving stability of functional protein fibrils
    • Griffith Jones, O. & Mezzenga, R. Inhibiting, promoting, and preserving stability of functional protein fibrils. Soft Matter 8, 876-895 (2012).
    • (2012) Soft Matter , vol.8 , pp. 876-895
    • Griffith Jones, O.1    Mezzenga, R.2
  • 13
    • 0037168655 scopus 로고    scopus 로고
    • A structural model for Alzheimer's b-amyloid fibrils based on experimental constraints from solid state NMR
    • Petkova, A. T. et al. A structural model for Alzheimer's b-amyloid fibrils based on experimental constraints from solid state NMR. Proc. Natl Acad. Sci. USA 99, 16742-16747 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16742-16747
    • Petkova, A.T.1
  • 14
    • 49649098999 scopus 로고    scopus 로고
    • Halogen versus hydrogen
    • Metrangolo, P. & Resnati, G. Halogen versus hydrogen. Science 321, 918-919 (2008).
    • (2008) Science , vol.321 , pp. 918-919
    • Metrangolo, P.1    Resnati, G.2
  • 16
    • 84872242097 scopus 로고    scopus 로고
    • Hydrogels of halogenated Fmoc-short peptides for potential application in tissue engineering
    • Wang, Y., Zhang, Z., Xu, L., Li, X. & Chen, H. Hydrogels of halogenated Fmoc-short peptides for potential application in tissue engineering. Colloids Surf. B Biointerfaces 104, 163-168 (2013).
    • (2013) Colloids Surf. B Biointerfaces , vol.104 , pp. 163-168
    • Wang, Y.1    Zhang, Z.2    Xu, L.3    Li, X.4    Chen, H.5
  • 17
    • 33645522802 scopus 로고    scopus 로고
    • Designed aromatic homo-dipeptides: Formation of ordered nanostructures and potential nanotechnological applications
    • Reches, M. & Gazit, E. Designed aromatic homo-dipeptides: formation of ordered nanostructures and potential nanotechnological applications. Phys. Biol. 3, S10-S19 (2006).
    • (2006) Phys. Biol. , vol.3 , pp. S10-S19
    • Reches, M.1    Gazit, E.2
  • 18
    • 33751322325 scopus 로고    scopus 로고
    • Halogen bonding and other noncovalent interactions involving halogens: A terminology issue
    • Metrangolo, P., Pilati, T. & Resnati, G. Halogen bonding and other noncovalent interactions involving halogens: a terminology issue. Cryst. Eng. Comm. 8, 946-947 (2006).
    • (2006) Cryst. Eng. Comm. , vol.8 , pp. 946-947
    • Metrangolo, P.1    Pilati, T.2    Resnati, G.3
  • 19
    • 79953235459 scopus 로고    scopus 로고
    • Effect of C-terminal modification on the self-assembly and hydrogelation of fluorinated Fmoc-Phe derivatives
    • Ryan, D. M., Doran, T. M., Anderson, S. B. & Nilsson, B. L. Effect of C-terminal modification on the self-assembly and hydrogelation of fluorinated Fmoc-Phe derivatives. Langmuir 27, 4029-4039 (2011).
    • (2011) Langmuir , vol.27 , pp. 4029-4039
    • Ryan, D.M.1    Doran, T.M.2    Anderson, S.B.3    Nilsson, B.L.4
  • 20
    • 77954576279 scopus 로고    scopus 로고
    • The influence of side-chain halogenation on the self-assembly and hydrogelation of Fmoc-phenylalanine derivatives
    • Ryan, D. M., Anderson, S. B. & Nilsson, B. L. The influence of side-chain halogenation on the self-assembly and hydrogelation of Fmoc-phenylalanine derivatives. Soft Matter 6, 3220-3231 (2010).
    • (2010) Soft Matter , vol.6 , pp. 3220-3231
    • Ryan, D.M.1    Anderson, S.B.2    Nilsson, B.L.3
  • 21
    • 84881059458 scopus 로고    scopus 로고
    • Definition of the halogen bond (IUPAC Recommendations 2013)
    • Desiraju, G. R. et al. Definition of the halogen bond (IUPAC Recommendations 2013). Pure Appl. Chem. 85, 1711-1713 (2013).
    • (2013) Pure Appl. Chem. , vol.85 , pp. 1711-1713
    • Desiraju, G.R.1
  • 23
    • 84899798295 scopus 로고    scopus 로고
    • Type II halogen - halogen contacts are halogen bonds
    • Metrangolo, P. & Resnati, G. Type II halogen - halogen contacts are halogen bonds. IUCrJ 1, 5-7 (2014).
    • (2014) IUCrJ , vol.1 , pp. 5-7
    • Metrangolo, P.1    Resnati, G.2
  • 24
    • 0023818388 scopus 로고
    • Calcitonin-like immunoreactivity of amyloid fibrils in medullary thyroid carcinomas. An immunoelectron microscope study. Virchows Arch
    • Berger, G., Berger, N., Guillaud, M. H., Trouillas, J. & Vauzelle, J. L. Calcitonin-like immunoreactivity of amyloid fibrils in medullary thyroid carcinomas. An immunoelectron microscope study. Virchows Arch. A Pathol. Anat. Histopathol. 412, 543-551 (1988).
    • (1988) A Pathol. Anat. Histopathol. , vol.412 , pp. 543-551
    • Berger, G.1    Berger, N.2    Guillaud, M.H.3    Trouillas, J.4    Vauzelle, J.L.5
  • 25
    • 0027480757 scopus 로고
    • The structure and mechanism of formation of human calcitonin fibrils
    • Arvinte, T., Cudd, A. & Drake, A. F. The structure and mechanism of formation of human calcitonin fibrils. J. Biol. Chem. 268, 6415-6422 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 6415-6422
    • Arvinte, T.1    Cudd, A.2    Drake, A.F.3
  • 26
    • 78751557975 scopus 로고    scopus 로고
    • Supramolecular gel chemistry: Developments over the last decade
    • Steed, J. W. Supramolecular gel chemistry: developments over the last decade. Chem. Commun. 47, 1379-1383 (2011).
    • (2011) Chem. Commun. , vol.47 , pp. 1379-1383
    • Steed, J.W.1
  • 27
    • 84871577538 scopus 로고    scopus 로고
    • Halogen-bonding-triggered supramolecular gel formation
    • Meazza, L. et al. Halogen-bonding-triggered supramolecular gel formation. Nat. Chem. 5, 42-47 (2013).
    • (2013) Nat. Chem. , vol.5 , pp. 42-47
    • Meazza, L.1
  • 28
    • 84872201218 scopus 로고    scopus 로고
    • Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis
    • Lakshmanana, A. et al. Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis. Proc. Natl Acad. Sci. USA 110, 519-524 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 519-524
    • Lakshmanana, A.1
  • 29
    • 77953906043 scopus 로고    scopus 로고
    • Specific mutations alter fibrillation kinetics, fiber morphologies, and membrane interactions of pentapeptides derived from human calcitonin
    • Shtainfeld, A., Sheynis, T. & Jelinek, R. Specific mutations alter fibrillation kinetics, fiber morphologies, and membrane interactions of pentapeptides derived from human calcitonin. Biochemistry 49, 5299-5307 (2010).
    • (2010) Biochemistry , vol.49 , pp. 5299-5307
    • Shtainfeld, A.1    Sheynis, T.2    Jelinek, R.3
  • 30
    • 79952158815 scopus 로고    scopus 로고
    • Natural tri-to hexapeptides self-assemble in water to amyloid b-type fiber aggregates by unexpected a-helical intermediate structures
    • Hauser, C. A. E. et al. 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 108, 1361-1366 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 1361-1366
    • Hauser, C.A.E.1
  • 31
    • 79958780734 scopus 로고    scopus 로고
    • Ultrasmall natural peptides self-assemble to strong temperature-resistant helical fibers in scaffolds suitable for tissue engineering
    • Mishra, A. et al. Ultrasmall natural peptides self-assemble to strong temperature-resistant helical fibers in scaffolds suitable for tissue engineering. Nano Today 6, 232-239 (2011).
    • (2011) Nano Today , vol.6 , pp. 232-239
    • Mishra, A.1
  • 33
    • 77955230701 scopus 로고    scopus 로고
    • Understanding amyloid aggregation by statistical analysis of atomic force microscopy images
    • Adamcik, J. et al. Understanding amyloid aggregation by statistical analysis of atomic force microscopy images. Nat. Nanotechnol. 5, 423-428 (2010).
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 423-428
    • Adamcik, J.1
  • 34
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • Nilsson, M. R. Techniques to study amyloid fibril formation in vitro. Methods 34, 151-160 (2004).
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1
  • 35
    • 84881247377 scopus 로고    scopus 로고
    • Distinct b-sheet structure in protein aggregates determined by ATR-FTIR spectroscopy
    • Shivu, B. et al. Distinct b-sheet structure in protein aggregates determined by ATR-FTIR spectroscopy. Biochemistry 52, 5176-5183 (2013).
    • (2013) Biochemistry , vol.52 , pp. 5176-5183
    • Shivu, B.1
  • 36
    • 84906085823 scopus 로고    scopus 로고
    • Orthogonal halogen and hydrogen bonds involving a peptide bond model
    • Vasylyeva, V. et al. Orthogonal halogen and hydrogen bonds involving a peptide bond model. Cryst. Eng. Comm. 16, 8102-8105 (2014).
    • (2014) Cryst. Eng. Comm. , vol.16 , pp. 8102-8105
    • Vasylyeva, V.1
  • 37
    • 0034643913 scopus 로고    scopus 로고
    • Infrared and Raman analyses of the halogen-bonded non-covalent adducts formed by a-$-diiodoperfluoroalkanes with DABCO and other electron donors
    • Messina, M. T. et al. Infrared and Raman analyses of the halogen-bonded non-covalent adducts formed by a-$-diiodoperfluoroalkanes with DABCO and other electron donors. J. Mol. Struct. 524, 87-94 (2000).
    • (2000) J. Mol. Struct. , vol.524 , pp. 87-94
    • Messina, M.T.1
  • 38
    • 0033830339 scopus 로고    scopus 로고
    • Myeloperoxidase and protein oxidation in cystic fibrosis
    • Vliet, V. D. et al. Myeloperoxidase and protein oxidation in cystic fibrosis. Am. J. Physiol. Lung Cell. Mol. Physiol. 279, L537-L546 (2000).
    • (2000) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.279 , pp. L537-L546
    • Vliet, V.D.1
  • 39
    • 0030979720 scopus 로고    scopus 로고
    • 3-chlorotyrosine, a specific marker of myeloperoxidase? Catalyzed oxidation is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima
    • Hazen, S. L. 3-chlorotyrosine, a specific marker of myeloperoxidase? Catalyzed oxidation is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima. J. Clin. Invest. 99, 2075-2075 (1997).
    • (1997) J. Clin. Invest. , vol.99 , pp. 2075-2075
    • Hazen, S.L.1
  • 40
    • 0035834065 scopus 로고    scopus 로고
    • Neutrophils employ the myeloperoxidase system to generate antimicrobial brominating and chlorinating oxidants during sepsis
    • Gaut, J. P. Neutrophils employ the myeloperoxidase system to generate antimicrobial brominating and chlorinating oxidants during sepsis. Proc. Natl Acad. Sci. USA 98, 11961-11961 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 11961-11961
    • Gaut, J.P.1
  • 41
    • 0034033812 scopus 로고    scopus 로고
    • Eosinophils generate brominating oxidants in allergen-induced asthma
    • Wu, W. et al. Eosinophils generate brominating oxidants in allergen-induced asthma. J. Clin. Invest. 105, 1455-1463 (2000).
    • (2000) J. Clin. Invest. , vol.105 , pp. 1455-1463
    • Wu, W.1
  • 42
    • 77955899792 scopus 로고    scopus 로고
    • Oxidative stress and protein deposition diseases in protein misfolding, aggregation, and conformational diseases
    • Mazzulli, J. R., Hodara, R., Lind, S. & Ischiropoulos, H. Oxidative stress and protein deposition diseases in protein misfolding, aggregation, and conformational diseases. Prot. Rev. 4, 123-133 (2006).
    • (2006) Prot. Rev. , vol.4 , pp. 123-133
    • Mazzulli, J.R.1    Hodara, R.2    Lind, S.3    Ischiropoulos, H.4
  • 43
    • 80052232617 scopus 로고    scopus 로고
    • Complementary p-p interactions induce multicomponent coassembly into functional fibrils
    • Ryan, D. M., Doran, T. M. & Nilsson, B. L. Complementary p-p interactions induce multicomponent coassembly into functional fibrils. Langmuir. 27, 11145-11156 (2011).
    • (2011) Langmuir. , vol.27 , pp. 11145-11156
    • Ryan, D.M.1    Doran, T.M.2    Nilsson, B.L.3
  • 44
    • 84963936091 scopus 로고    scopus 로고
    • Searching sequence space
    • Gazit, E. Searching sequence space. Nat. Chem. 7, 14-15 (2015).
    • (2015) Nat. Chem. , vol.7 , pp. 14-15
    • Gazit, E.1
  • 45
    • 84963944295 scopus 로고    scopus 로고
    • Exploring the sequence space for (tri-)peptide selfassembly to design and discover new hydrogels
    • Frederix, P. W. J. M. et al. Exploring the sequence space for (tri-)peptide selfassembly to design and discover new hydrogels. Nat. Chem. 7, 30-37 (2015).
    • (2015) Nat. Chem. , vol.7 , pp. 30-37
    • Frederix, P.W.J.M.1
  • 47
    • 40849136136 scopus 로고    scopus 로고
    • Mercury CSD 2.0-new features for the visualization and investigation of crystal structures
    • Macrae, C. F. et al. Mercury CSD 2.0-new features for the visualization and investigation of crystal structures. J. Appl. Cryst. 41, 466-470 (2008).
    • (2008) J. Appl. Cryst. , vol.41 , pp. 466-470
    • Macrae, C.F.1
  • 49
    • 84888630744 scopus 로고    scopus 로고
    • Halogen interactions in protein-ligand complexes: Implications of halogen bonding for rational drug design
    • Sirimulla, S., Bailey, J. B., Vegesna, R. & Narayan, M. Halogen interactions in protein-ligand complexes: implications of halogen bonding for rational drug design. J. Chem. Inf. Model. 53, 2781-2791 (2013).
    • (2013) J. Chem. Inf. Model. , vol.53 , pp. 2781-2791
    • Sirimulla, S.1    Bailey, J.B.2    Vegesna, R.3    Narayan, M.4
  • 50
    • 30344453639 scopus 로고    scopus 로고
    • Triangular halogen trimers. A DFT study of the structure, cooperativity, and vibrational properties
    • Lu, Y. et al. Triangular halogen trimers. A DFT study of the structure, cooperativity, and vibrational properties. J. Phys. Chem. A 109, 11956-11961 (2005).
    • (2005) J. Phys. Chem. A , vol.109 , pp. 11956-11961
    • Lu, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.