Inhibition ofβ-Amyloid Aggregation and Neurotoxicity by Complementary (Antisense) Peptides

Heal, Jonathan R.; Roberts, Gareth W.; Christie, Gary; Miller, Andrew D.

doi:10.1002/1439-7633(20020104)3:1<86::aid-cbic86>3.0.co;2-l

Cited by 18 publications

(17 citation statements)

References 27 publications

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“…(anti)-idiotypic antibodies [100,101] insulin [102] integrin [103] IFN-g [104] IFN-b [105] IL-1b IL-2 IL-18 [10,11,13,106,107] [108,109] [12] laminin receptor [110] luteinising hormone-releasing hormone [18,111] melanocyte stimulating hormone MHC II/peptide antigens [112] [113] trypsin-modulating oostatic factor [114] myelin basic protein neurokinin A/tachykinin NK1 receptor [33] [ 115] neurophysin II neutrophil chemoattractant nitric oxide synthase [77,116] [117] [118] ovine prolactin bovine P2 protein [119] [ 32] prion protein [120] ribonuclease S-peptide SARS-CoV protein [121,122] [ 36] somatostatin [123] substance P [23] T15 self-binding antibody thrombospondin-1/latency-associated peptide (LAP) TNF-a [26] [124] [125] vitronectin [93] (complementary) peptide mini-receptor inhibitors may be used to inhibit the aggregation of amyloid peptides, Ab, thereby significantly reducing Ab-mediated neurotoxicity [34]. Relatively recently, Imai et al demonstrated that HIV-1 infection can be modulated in vitro using antisense peptides that derive from internally complementary peptide sequences within the chemokine CCR5 receptor that otherwise participates with CD4 in mediating HIV-1 entry into white blood cells (leucocytes) [35].…”

Section: Extending the Applications Of Sense--antisense Peptide Intermentioning

confidence: 99%

“…Indeed, there are several pieces of evidence that are consistent with this suggestion too. For instance: 1) measured sense--antisense peptide interactions are characterised by K d values in the low µM region, so they are specific but not hugely strong [10][11][12]34,36]. Even though in biology such K d values are sufficient for certain transient interactions, binding interactions with K d values in the low nM region are routine [1]; 2) some M-I pairs remain difficult to understand because they involve amino acid residues that are hydropathic opposites, with hydrophilic residues pairing up with hydrophobic ones (Figure 4, Table 3), yet protein--protein interfaces are already known to possess substantial hydrophobic-hydrophobic amino acid residue contacts [ 3) Root-Bernstein has defined alternatives to the M-I pairs that arise by the reading of antisense codons in the 3¢ !…”

Section: Extending the M-i Pair Theory Of Interaction To The Proteomimentioning

confidence: 99%

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Sense–antisense (complementary) peptide interactions and the proteomic code; potential opportunities in biology and pharmaceutical science

Miller

2015

Expert Opinion on Biological Therapy

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Studies on the potential mechanism of sense-antisense peptide interactions suggest that interactions may be driven by amino acid residue interactions specified from the genetic code. If so, such specified amino acid residue interactions could form the basis for an even wider amino acid residue interaction code (proteomic code) that links gene sequences to actual protein structure and function, even entire genomes to entire proteomes. The possibility that such a proteomic code should exist is discussed. So too the potential implications for biology and pharmaceutical science are also discussed were such a code to exist.

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Section: Extending the Applications Of Sense--antisense Peptide Intermentioning

confidence: 99%

Section: Extending the M-i Pair Theory Of Interaction To The Proteomimentioning

confidence: 99%

Sense–antisense (complementary) peptide interactions and the proteomic code; potential opportunities in biology and pharmaceutical science

Miller

2015

Expert Opinion on Biological Therapy

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“…Nmethylmorpholine, piperidine, dichloromethane (DCM), N,N′-dimethylformamide (DMF) and epichlorohydrin were of analytical grade and purchased from Beijing Chemical Factory, China. Monodispersed non-porous poly(glycidyl methacrylate) beads (PGMA) containing active epoxy groups were home made [11] . Triple distilled water was used throughout.…”

Section: Chemicals and Samplesmentioning

confidence: 99%

“…Moreover, Davids et al [8] developed antisense peptides as the selective inhibitors of cytokine interleukin I in 1997. Since then, antisense peptides have been designed and selected as inhibitors of cytokine interleukin-1β [9] , interleukin 18 [10] and β-amyloid peptide 1-40 [11] . In our previous work, the inhibitor of influenza A virus was designed and screened out using antisense peptide based combinatorial peptide libraries [12] .…”

mentioning

confidence: 99%

Study on peptide-peptide interaction using high-performance affinity chromatography and quartz crystal microbalance biosensor

et al. 2007

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The specific interaction between sense and antisense peptides was studied by high-performance affinity chromatography (HPAC) and quartz crystal microbalance (QCM) biosensor. Fragment 1-14 of human interferon-β (hIFN-β) was chosen as sense peptide and its three antisense peptides (AS-IFN 1, AS-IFN 2, and AS-IFN 3) were designed according to the degeneracy of genetic codes. The affinity column was prepared with sense peptide as ligand and the affinity chromatographic behavior was evaluated. Glu-substituted antisense peptide (AS-IFN 3) showed the strongest binding to immobilized sense peptide at pH 7.5. A quartz crystal microbalance-flow injection analysis (QCM-FIA) system was introduced to investigate the recognition process in real-time. The equilibrium dissociation constants between sense peptide and AS-IFN 1, AS-IFN 2 and AS-IFN 3 measured 2.08×10 −4 , 1.31×10 −4 and 2.22× 10 −5 mol/L, respectively. The mechanism study indicated that the specific recognition between sense peptide and AS-IFN 3 was due to sequence-dependent and multi-modal affinity interaction.antisense peptide, degeneracy, high-performance affinity chromatography, quartz crystal microbalance biosensor, human interferon-β Antisense peptides are the analogical equivalent of antisense oligonucleotides. By definition, a sense peptide is coded by the nucleotide sequence of the sense (positive) strand of DNA. Conversely, an antisense peptide is coded by the nucleotide sequence of the antisense (negative) strand of DNA. Usually the antisense strand of DNA cannot be translated in almost all organisms, but they can be synthesized chemically. As predicted by Mekler [1] and first shown experimentally by Bost et al. [2] , an antisense peptide could interact with the corresponding sense peptide at some degree of selectivity. The interaction between sense and antisense peptides has been reported [3,4] . As such interaction is specific and selective, its application in affinity technology has been widely achieved. For example, antisense peptide-immobilized chromatographic supports have been employed to isolate native proteins like recombinant c-raf protein [5] , the Arg 8 -vasopressin-receptor complex [6] and human interferon-β [7] . Moreover, Davids et al. [8] developed antisense peptides as the selective inhibitors of cytokine interleukin I in 1997. Since then, antisense peptides have been designed and selected as inhibitors of cytokine interleukin-1β [9] , interleukin 18 [10] and β-amyloid peptide 1-40 [11] . In our previous work, the inhibitor of influenza A virus was designed and screened out using antisense peptide based combinatorial peptide libraries [12] .Till now, the mechanism of interactions between sense and antisense peptides has not been clarified. Two main hypotheses have been put forward to explain the specific interactions between sense peptide and antisense peptide. As defined by Heal et al. in 2002 [4] , one

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“…Antisense peptides derived from the mRNA of Aβ1-40 have also been designed to bind directly to Aβ [90]. Of the six complementary peptides synthesised, one showed specific binding to Aβ1-40 and inhibited fibrillogenesis and neurotoxicity.…”

Section: Peptide Aggregation Inhibitorsmentioning

confidence: 99%

Recent Developments in the Understanding and Treatment of Neurodegenerative Disorders Involving Protein Conformational Misfolding and Amyloid Formation

Thompson¹,

Barrow²

2005

MCRO

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Conformational disease represents an intriguing but devastating class of neurodegenerative disorders that includes prion disease, Alzheimer's disease, Parkinson's disease and Huntington's disease. Although symptoms, on-set times and prognosis among the diseases can vary markedly, the deposition of neurotoxic protein aggregates is a significant commonality, and as such is an attractive therapeutic target. Understanding the mechanisms of protein misfolding and deposition in these conditions is critical to developing effective diagnostic and therapeutic agents. This review serves as an update for the sister publication "Protein Conformational Misfolding and Amyloid Formation: Characteristics of a New Class of Disorders that Include Alzheimer's and Prion Diseases" in Curr. Med. Chem. 2002, 9, 1751, and focuses primarily on recent developments in understanding prion disease and Alzheimer's disease in context with other conformational disease. New research in amyloid-related therapeutic strategies is also discussed.

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Inhibition ofβ-Amyloid Aggregation and Neurotoxicity by Complementary (Antisense) Peptides

Cited by 18 publications

References 27 publications

Sense–antisense (complementary) peptide interactions and the proteomic code; potential opportunities in biology and pharmaceutical science

Sense–antisense (complementary) peptide interactions and the proteomic code; potential opportunities in biology and pharmaceutical science

Study on peptide-peptide interaction using high-performance affinity chromatography and quartz crystal microbalance biosensor

Recent Developments in the Understanding and Treatment of Neurodegenerative Disorders Involving Protein Conformational Misfolding and Amyloid Formation

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