Analysis amyloid

These results indicate that is it possible to change the fold of a protein by changing a restricted set of residues. They also confirm the validity of the rules for stability of helical folds that have been obtained by analysis of experimentally determined protein structures. One obvious impliction of this work is that it might be possible, by just changing a few residues in Janus, to design a mutant that flip-flops between a helical and p sheet structures. Such a polypeptide would be a very interesting model system for prions and other amyloid proteins. 

Shen CL, Scott GL, Merchant F, Murphy RM. Light scattering analysis of fibril growth from the amino-terminal fragment beta(l-28) of beta-amyloid peptide. Biophys J 1993 65 2383-2395. 

Inouye H, Fraser PE, Kirschner DA. Structure of beta-crystalline assemblies formed by Alzheimer beta-amyloid protein analogues analysis by X-ray diffraction. Biophys J 1993 64 502-519. 

The molecular structure of the amyloid fibrils formed by fragment 105-115 of transthyretin (TTR10sns, YTIAALLSPTS) has been characterized by solid-state NMR. The fibril backbone structure was first established based on the TALOS analysis of the 15N and 13C chemical shifts [89]. Using the correlation experiments of Hn(0-N(0—CV-H0 , Ha(0-Ca(0-N(i.+1)-HN(i+1), and N -Tco-N, a total of 41 constraints on 19 backbone torsion angles have been obtained in a... 

The contributions to this volume demonstrate that structural studies of fibrous /1-proteins, as well as prion and amyloid fibrils, have advanced rapidly thanks in large part to improved experimental techniques and better theoretical analysis of the ever-increasing structural data. It is also possible to learn from studies of naturally occurring silks (Dicko et al., this volume) howvariations in the conditions of production of silk threads from the same protein can produce a variety of /1-structures with very distinct... 

Cannon, M. J., Williams, A. D., Wetzel, R., and Myszka, D. G. (2004). Kinetic analysis of beta-amyloid fibril elongation. Anal. Biochem. 328, 67-75. 

Amyloid fibrils form from a variety of native proteins with diverse sequences and folds. The classic method for the structural analysis of amyloid has been X-ray fiber diffraction amyloid fibrils exhibit a characteristic diffraction signature, called the cross-/) pattern. This cross-/ pattern suggested a repeating structure in which /1-sheets run parallel to the fiber axis with their constituent /1-strands perpendicular to that direction (Sunde and Blake, 1997). This diffraction signature pointed to an underlying common core molecular structure for the amyloid fibril that could accommodate diverse sequences and folds. A number of groups have proposed amyloid folds that are consistent with the experimental data and these can be linked to repeating /1-structured units. 

Zhu, L., Zhang, X. J., Wang, L. Y., Zhou, J. M., and Perrett, S. (2003). Relationship between stability of folding intermediates and amyloid formation for the yeast prion Ure2p A quantitative analysis of the effects of pH and buffer system./ Mol. Biol. 328, 235-254. 

Inouye, H., Fraser, P. E., and Kirschner, D. A. (1993). Structure of //-crystallite assemblies formed by Alzheimer //-amyloid protein analogues Analysis by x-ray diffraction. Biophys.J. 64, 502-519. 

Mason, R. P., Estermyer, J. D., Kelly, J. F., and Mason, P. E. (1996). Alzheimer s disease amyloid // peptide 25-35 is localized in the membrane hydrocarbon core X-ray diffraction analysis. Biochem. Biophys. Res. Commun. 222, 78-82. 

Shirahama, T., and Cohen, A. S. (1967). High-resolution electron microscopic analysis of the amyloid fibril./ Cell Biol. 33, 679-708. 

McPhie, P. (2004). CD studies on films of amyloid proteins and polypeptides Quantitative g-factor analysis indicates a common folding motif. Biopolymers 75, 140-147. 

Roterman, I., KrUl, M., Nowak, M., Konieczny, L., Rybarska, J., Stopa, B., Piekarska, B., and Zemanek, G. (2001). Why Congo red binding is specific for amyloid proteins— model studies and a computer analysis approach. Med. Sci. Mcmit. 7, 771-784. 

Shanmugam, G., andjayakumar, R. (2004). Structural analysis of amyloid beta peptide fragment (25—35) in different microenvironments. Biopolymers 76, 421—134. 

Several additional useful publications demonstrating practical applications of CE/MS methods for neurotransmitter analysis and neuropharmaceutical studies are those of Larsson and Lutz (2000) (neuropeptides including substance P) Hettiarachchi et al. (2001) (synthetic opioid peptides) Varesio et al. (2002) (amyloid-beta peptide) Zamfir and Peter-Katalinic (2004) (gangliosides) Peterson et al. (2002) (catecholamines and metanephrines) Cherkaoui and Veuthey (2002) (fluoxetine) and Smyth and Brooks (2004) (various lower molecular weight molecules including benzodiazepines, steroids, and cannabinols). 

Takahashi Y, Ueno A, Mihara H. Mutational analysis of designed peptides that undergo stmctural transition fi om a helix to /3 sheet and amyloid fibril formation. Structure 2000 8 915-925. 

N.M. Kemppainen, S. Aalto, I.A. Wilson, K. Nagren, S. Helin, A. Bruck, V. Oikonen, M. Kailajarvi, M. Scheinin, M. Viitanen, R. Parkkola, J.O. Rinne, Voxel-based analysis of amyloid ligand [ C]PIB uptake in Alzheimer disease, Neurology 67 (2006) 1575-1580. 

Amyloid fibrils formed from a-synuclein have been found in Lewy bodies of patients with Parkinson s disease.64 Spin labels were introduced at 36 positions between amino acid 5 and 136 of a-synuclein. Distributions of interspin distances between the same labels on neighboring chains were determined by analysis of CW line-shapes in solution. For the fibrils analysis of the percent of molecules with distances <15 A, 15-20 A, and > 20 A revealed a highly ordered and specifically folded core region of 70 amino acids ( residues 34 to 101). In contrast, the N terminus region is structurally heterogeneous and the C terminus appears to be completely unfolded. 

ICP-MS has been combined with flow injection and a selective extraction procedure (which isolates Alzheimer s amyloid plaques) for the selective analysis of plaque cores.103 The results of multi-element analysis indicate the accumulation of several elements (Al, Fe, Zn) in the plaques. 

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