Location of .beta.-sheet-forming sequences in amyloid proteins by FTIR

Halverson, Kurt J.; Sucholeiki, Irving; Ashburn, Ted T.; Lansbury, Peter T.

doi:10.1021/ja00017a068

Cited by 141 publications

(282 citation statements)

References 0 publications

Supporting

Mentioning

252

Contrasting

Unclassified

Order By: Relevance

“…Amyloid ␤ fragment 25-35 (A␤ [25][26][27][28][29][30][31][32][33][34][35] ) ( Figure 1A) and scrambled A␤ [25][26][27][28][29][30][31][32][33][34][35] peptides (NeoMPS, Strasbourg, France) were dissolved in sterile bidistilled water at 1 g/ L concentration (soluble form) and were stored at Ϫ20°C. The scrambled A␤ [25][26][27][28][29][30][31][32][33][34][35] and A␤ [25][26][27][28][29][30][31][32][33][34][35] peptides were aggregated by in vitro incubation at 37°C for 4 days.…”

Section: Amyloid ␤ Peptidementioning

confidence: 99%

“…4 Structure-activity studies revealed that peptides containing the highly hydrophobic 25-35 region formed stable aggregates and mediated neuronal death by necrosis or apoptosis. 5,6,7 The truncated A␤ [25][26][27][28][29][30][31][32][33][34][35] fragment includes extracellular and intramembrane residues that have been reported to represent an active region of A␤. 8 In vivo, two nontransgenic rodent models of AD have been studied to analyze the molecular, morphological, and behavioral consequences of amyloid toxicity: the infusion of A␤ 1-40/42 protein and the injection of preaggregated A␤ [25][26][27][28][29][30][31][32][33][34][35] peptide.…”

mentioning

confidence: 99%

“…These models have led to highly pertinent pathomimetic observations and provide complementary approaches to the numerous transgenic mouse lines developed as AD models. In particular, at 1 week after A␤ [25][26][27][28][29][30][31][32][33][34][35] injection, reactive gliosis was observed in the rat hippocampus, 9 caspase-3 activity was induced in the hippocampus and cortex, 9 a reduction in the number of neurons was measured in the CA1 or CA3 hippocampal area, 9 -11 and significant oxidative stress was observed. [11][12][13] Nonetheless, this amyloid toxicity model remains controversial with respect to AD.…”

mentioning

confidence: 99%

“…First, although the presence of A␤ [25][26][27][28][29][30][31][32][33][34][35] has been repeatedly demonstrated in brains of AD patients, 14,15 this fragment appears to be a minor peptide in plaques and its contribution to the toxicity induced by all amyloid-related species remains unclear. Second, the intracerebroventricular injection of A␤ [25][26][27][28][29][30][31][32][33][34][35] induces marked toxicity within days or weeks, which is not in accord with the long-term progression of AD in humans (an argument that is unrelated to the nature of the toxicity). Third, it is possible that peptide injection mimics only the amyloid toxicity observed in AD physiopathology, but not the processes involved in A␤ formation or Tau protein hyperphosphorylation.…”

mentioning

confidence: 99%

“…Klementiev et al 16 recently documented some evidence that contradicts this latter reservation. Moreover, very recently, Chavant et al 17 reported that, at 2 weeks after injection, A␤ [25][26][27][28][29][30][31][32][33][34][35] significantly increased APP processing in the hippocampus of mice.…”

mentioning

confidence: 99%

See 4 more Smart Citations

Time-Course and Regional Analyses of the Physiopathological Changes Induced after Cerebral Injection of an Amyloid β Fragment in Rats

Zussy

Brureau

Delair

et al. 2011

The American Journal of Pathology

116

129

View full text Add to dashboard Cite

Alzheimer's disease (AD) is a neurodegenerative pathology characterized by the presence of senile plaques and neurofibrillary tangles, accompanied by synaptic and neuronal loss. The major component of senile plaques is an amyloid ␤ protein (A␤) formed by pathological processing of the A␤ precursor protein. We assessed the time-course and regional effects of a single intracerebroventricular injection of aggregated A␤ fragment 25-35 (A␤ 25-35 ) in rats. Using a combined biochemical, behavioral, and morphological approach, we analyzed the peptide effects after 1, 2, and 3 weeks in the hippocampus, cortex, amygdala, and hypothalamus. The scrambled A␤ 25-35 peptide was used as negative control. The aggregated forms of A␤ peptides were first characterized using electron microscopy, infrared spectroscopy, and Congo Red staining. Intracerebroventricular injection of A␤ 25-35 decreased body weight, induced short-and long-term memory impairments, increased endocrine stress, cerebral oxidative and cellular stress, neuroinflammation, and neuroprotective reactions, and modified endogenous amyloid processing, with specific time-course and regional responses. Moreover, A␤ 25-35 , the presence of which was shown in the different brain structures and over 3 weeks, provoked a rapid glial activation, acetylcholine homeostasis perturbation, and hippocampal morphological alterations. Alzheimer's disease (AD) is a chronic neurodegenerative pathology characterized by the presence of senile plaques and neurofibrillary tangles, accompanied by synaptic and neuronal loss in brain areas responsible for learning and memory impairments. 1 The major component of senile plaques is an amyloid ␤ protein (A␤) derived from amyloid precursor protein (APP). Genetic, cell biological, and postmortem studies on AD brain, together with A␤ neurotoxicity findings, gave rise to the amyloid cascade hypothesis to explain A␤-associated neurodegenerative processes. 2 In normal healthy individuals, A␤ peptides are present only in small quantities, as soluble monomers that circulate in cerebrospinal fluid and blood. In AD patients, A␤ peptides, which vary in length from 40 to 43 amino acids, accumulate as insoluble fibrillar deposits. 3 When cultured rat hippocampal neurons are exposed to aggregated A␤ peptides, their neurites adopt a dystrophic appearance and become comparable to those observed surrounding and infiltrating senile plaques. This observation suggested that A␤ is responsible for the neuritic abnormalities in AD pathology. 4 Structure-activity studies revealed that peptides containing the highly hydrophobic 25-35 region formed stable aggregates and mediated neuronal death by necrosis or apoptosis. 5,6,7 The truncated A␤ 25-35 fragment includes extracellular and intramembrane residues that have been reported to represent an active region of A␤. 8

show abstract

Section: Amyloid ␤ Peptidementioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Time-Course and Regional Analyses of the Physiopathological Changes Induced after Cerebral Injection of an Amyloid β Fragment in Rats

Zussy

Brureau

Delair

et al. 2011

The American Journal of Pathology

116

129

View full text Add to dashboard Cite

show abstract

Infrared Spectroscopy of Proteins

Fabian

Mäntele

2001

Handbook of Vibrational Spectroscopy

114

130

View full text Add to dashboard Cite

Infrared spectroscopy provides molecular information in systems that range from the level of peptides, isolate proteins and enzymes, to even more complex systems such as peptide–protein complexes and membrane‐bound proteins. The information may be a global one such as the secondary structure composition of a protein, or it may be highly specific such as the alteration of individual vibrating bonds in an enzyme. Furthermore, the structural information is not restricted to a static picture, but can also be obtained at high time resolution to allow true structure–function correlation. Illustrative examples are given to demonstrate the sort of information, which infrared techniques can provide and how this information can be extracted from the experimental data. In addition, strengths and limitations of the infrared approach are discussed. This should help the reader to evaluate whether a particular system is appropriate for study by infrared spectroscopy, and what specific advantages are gained when applying infrared techniques.

show abstract

IR spectroscopy of isotope-labeled helical peptides: Probing the effect of N-acetylation on helix stability

Decatur

2000

Biopolymers

131

View full text Add to dashboard Cite

The effect of N‐acetylation on the conformation of alanine‐rich helical peptides is examined using isotope‐edited Fourier transform infrared (FTIR) spectroscopy. A series of peptides with sequence AA(AAKAA)3AAY has been prepared; each peptide incorporates four 13C‐labeled alanines. These peptides have two amide I′ bands in their FTIR spectra: one corresponding to the 12C amino acids, and one assigned to the 13C amino acids. The intensity and frequency of the 13C amide I′ band varies systematically with the position of the labels in the sequence and the presence or absence of an N‐acetyl capping group. The intensity of the 13C amide I′ band correlates with helix stability at the labeled residues as predicted by thermodynamic models of the helix–coil transition. These results suggest that FTIR spectroscopy combined with specific isotope labeling can be used to dissect the conformation of helical peptides at the residue level. © 2000 John Wiley & Sons, Inc. Biopoly 54: 180–185, 2000

show abstract

Location of .beta.-sheet-forming sequences in amyloid proteins by FTIR

Cited by 141 publications

References 0 publications

Time-Course and Regional Analyses of the Physiopathological Changes Induced after Cerebral Injection of an Amyloid β Fragment in Rats

Time-Course and Regional Analyses of the Physiopathological Changes Induced after Cerebral Injection of an Amyloid β Fragment in Rats

Infrared Spectroscopy of Proteins

IR spectroscopy of isotope-labeled helical peptides: Probing the effect of N-acetylation on helix stability

Contact Info

Product

Resources

About