Peptides
Products for Peptides
- Cat.No. Product Name Information
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GC62017
α-CGRP, rat TFA
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GC62016
α-Conotoxin AuIB TFA
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GC38042
α-Factor Mating Pheromone, yeast (TFA)
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GC63270
α-Glucosidase
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GC63271
α-Synuclein (61-75) (TFA)
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GC38873
α2β1 Integrin Ligand Peptide TFA
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GC37984
β-Amyloid (1-42), rat
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GC61394
β-Amyloid (1-42), rat TFA
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GC61988
β-amyloid (12-28) (TFA)
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GC39466
β-Amyloid 15-21
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GC37991
β-Amyloid 15-21
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GC38003
β-Casomorphin (1-5), bovine
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GC60391
β-Casomorphin, bovine TFA
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GC61484
β-Casomorphin, human TFA
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GC34944
β-CGRP, human TFA
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GC45230
β-Defensin-3 (human) (trifluoroacetate salt)
β-Defensin-3 is a peptide with antimicrobial properties that protects the skin and mucosal membranes of the respiratory, genitourinary, and gastrointestinal tracts.
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GC45231
β-Defensin-4 (human) (trifluoroacetate salt)
β-Defensin-4 is a peptide with antimicrobial properties that protects the skin and mucosal membranes of the respiratory, genitourinary, and gastrointestinal tracts.
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GC45234
β-Endorphin (1-27) (human) (trifluoroacetate salt)
β-Endorphin (1-27) is an endogenous peptide that binds to μ-, δ-, and κ-opioid receptors (Kis = 5.31, 6.17, and 39.82 nM, respectively, in COS-1 cells expressing rat receptors).
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GC45236
β-Endorphin (rat)
β-Endorphin (β-EP) is an endogenous opioid neuropeptide with diverse biological activities.
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GC38030
β-Endorphin, equine (TFA)
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GC38007
β-Melanocyte Stimulating Hormone (MSH), human TFA
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GC61462
γ-1-Melanocyte Stimulating Hormone (MSH), amide
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GC62081
γ-Glu-Phe TFA
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GC17002
γ1-MSH
melanocortin MC3 receptor agonist
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GC15513
ω-Agatoxin IVA
P-type calcium channels blocker
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GC12608
ω-Agatoxin TK
CaV2.1 P/Q-type calcium channels blocker
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GC13886
ω-Conotoxin GVIA
blocker of N-type calcium channels
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GC18070
ω-Conotoxin MVIIC
wide spectrum blocker of N, P and Q type calcium channels
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GC10426
α-Bungarotoxin
α7 nAChR antagonist
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GC15519
α-CGRP (human)
Endogenous calcitonin gene-related peptide receptor (CGRP) agonist
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GC10872
α-Conotoxin AuIB
Selective antagonist of α3β4 nicotinic acetylcholine receptors
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GC14296
α-Conotoxin PIA
Selective antagonist of α6-containing nicotinic receptors
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GC10368
α-Conotoxin PnIA
Selective antagonist of α3β2 nAChR receptors
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GC30587
α-Factor Mating Pheromone, yeast (Mating Factor α)
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GC11346
α-helical CRF 9-41
Antagonist of corticotropin releasing factor receptor
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GC34242
β-Amyloid (1-42), rat TFA
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GC31146
β-Amyloid (10-35), amide
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GC31129
β-Amyloid 1-16 (Amyloid β-Protein (1-16))
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GC31171
β-Amyloid 1-28 (Amyloid β-Protein (1-28))
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GC30325
β-Amyloid 22-35 (Amyloid β-Protein (22-35))
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GC31137
β-Amyloid 29-40 (Amyloid beta-protein(29-40))
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GC31179
β-Amyloid 31-35
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GC33736
β-Casomorphin, bovine (β-Casomorphin-7 (bovine))
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GC33784
β-Casomorphin, human (Human β-casomorphin 7)
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GC33585
β-catenin peptide
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GC33595
β-CGRP, human (Human β-CGRP)
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GC33693
β-Melanocyte Stimulating Hormone (MSH), human (Beta-MSH (1-22) (human))
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GC31172
δ-Sleep Inducing Peptide (Delta-Sleep Inducing Peptide)
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GC30187
γ-Glu-Phe (γ-Glutamylphenylalanine)
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GC62067
ω-Conotoxin GVIA TFA
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GA24016
ω-Conotoxin MVIIA
ω-Conotoxin MVIIA, originally isolated from the venom of the fish-hunting cone snail Conus magus, is a blocker of voltage-sensitive Ca²? channels in neurons. The peptide has been used to identify different Ca²? channel subtypes in amphibian brain.
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GA20024
(7-Diethylaminocoumarin-3-yl)carbonyl-Amyloid β-Protein (1-40)
Amyloid β-protein (1-40) that is N-terminally modified with the fluorescent dye (7-diethylaminocoumarin-3-yl)carbonyl (DAC or DEAC). This derivative can be utilized to assess the binding properties of amyloid β-protein (1-40) for various membranes since it behaves very similar to the native peptide. In aqueous environments the fluorophore is almost non-fluorescent whereas binding to membranes results in an increase in fluorescence intensity (Λex = 430 nm, Λem = 470 nm). Increases in the GM1 ganglioside and cholesterol content in the lipid bilayers facilitated the binding of this peptide. For phosphatidylcholine and phosphatidylserine no affinity was observed.
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GA20029
(Arg¹³)-Amyloid β-Protein (1-40)
H13R, a mutation in the metal-binding region of Abeta reduces its copper-mediated toxicity. The native rodent sequence containing an arginine at this position is more tolerant to metals than the human amyloid peptide.
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GC34977
(Arg)9 TFA
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GA20030
(Arg⁶)-Amyloid β-Protein (1-40)
The English (H6R) mutation of β-amyloid peptides accelerates fibrillation without increasing protofibril formation. Ono et al. showed that the English and Tottori mutations alter Abeta assembly at its earliest stages, monomer folding and oligomerization, and produce oligomers that are more toxic to cultured neuronal cells than are wild type oligomers.
The exchange of His? by Arg influences the structure of the Cu(II) complex formed by Aβ peptides.
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GA20038
(Asn²³)-Amyloid β-Protein (1-40)
The Iowa (D23N) mutant of Aβ 40 considerably more rapidly assembles in solution to form fibrils than the WT Aβ sequence. These fibrils also show a different structure, which could be responsible for their increased toxicity.
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GA20039
(Asn⁶⁷⁰,Leu⁶⁷¹)-Amyloid β/A4 Protein Precursor₇₇₀ (667-675)
SEVNLDAEF corresponds to the mutant junctional sequence of the amyloid precursor protein (APP) found in a Swedish family with early-onset Alzheimer's disease, therefore referred to as the 'Swedish' mutation (K670N/M671L). The peptide has been used for assaying cleavage at leucine-aspartate by cathepsin G and chymotrypsin, whereas neither cathepsin B, D nor L generated any products.
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GA20040
(Asn⁶⁷⁰,Leu⁶⁷¹)-Amyloid β/A4 Protein Precursor₇₇₀ (667-676)
This peptide substrate corresponds to the 'Swedish' Lys-Met/Asn-Leu (K670N/M671L) mutation of the amyloid precursor protein (APP) β-secretase cleavage site. It has been used for assaying β-secretase activity.
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GA20041
(Asn⁶⁷⁰,Sta⁶⁷¹,Val⁶⁷²)-Amyloid β/A4 Protein Precursor₇₇₀ (662-675)
Amyloid precursor protein (APP) β-secretase from human brain cleaves full-length APP at the amino terminus of the amyloid β-protein (Aβ) sequence, thus leading to the generation and extracellular release of β-cleaved soluble APP and a corresponding cell-associated carboxy-terminal fragment. The subsequent cleavage of the C-terminal fragment by γ-secretase(s) leads to the formation of Aβ. This new peptide represents a potent substrate analog inhibitor of APP β-secretase with IC?? = 30 nM.
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GA20042
(Asn⁷)-Amyloid β-Protein (1-40)
The Tottori (D7N) mutation of β-amyloid peptides accelerates fibrillation without increasing protofibril formation. Ono et al. showed that the English and Tottori mutations alter Abeta assembly at its earliest stages, monomer folding and oligomerization, and produce oligomers that are more toxic to cultured neuronal cells than are wild type oligomers.
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GA20045
(Asp³⁷)-Amyloid β-Protein (1-42)
The G37D mutant does not show the aggregation behavior of WT Abeta42 nor its neurotoxicity.
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GA20053
(Cys²⁶)-Amyloid β-Protein (1-40)
Aβ40 S26C has been used for generating the covalently linked Aβ40 homodimer. Dimerization can be easily reverted by reducing the soluble dimer with thiols as β-mercaptoethanol. Aβ40 S26C is perfectly suited for labeling with fluorescent tags
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GA20052
(Cys²⁶)-Amyloid β-Protein (1-40) (Dimer)
Dimer of H-7402.
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GA20050
(Cys⁰)-Amyloid β-Protein (1-40)
Cys-Aβ1-40 can be easily and selectively modified, labeled, coupled to carriers e.g. by maleimide chemistry without affecting the sequences involved in fibril formation. The free mercapto moiety of the peptide adheres to gold surfaces.
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GA20054
(Cys⁴⁷)-HIV-1 tat Protein (47-57)
CPP for gene delivery.
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GA20164
(D-Trp¹²,Tyr³⁴)-pTH (7-34) amide (bovine)
The D-Trp¹² substitution leads to a competitive pTH antagonist with increased inhibitory properties in vitro.
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GA20094
(Des-Cys¹,cyclo(Ser²-Asu⁷))-Calcitonin (eel)
Elcatonin, also known as carbocalcitonin, is the aminosuberic acid analog of eel calcitonin. It has all the biological properties of the corresponding natural calcitonin (H-2255). The substitution of the disulfide bond of natural calcitonins with an ethylene bridge in 1-7 N-terminal position gives elcatonin greater stability and excellent tolerability when used in vivo.
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GA20095
(Des-Glu²²)-Amyloid β-Protein (1-40)
The Osaka mutation was the first deletion-type mutation to be identified in APP and Aβ.
The Aβ E22delta mutant is more resistant to degradation by two major Aβ-degrading enzymes, neprilysin and insulin-degrading enzyme. Synthetic mutant Aβ showed unusual aggregation properties with enhanced oligomerization but no fibrillization. It also inhibited hippocampal long-term potentiation more efficiently than wild-type Aβ. A transgenic mouse model containing APP with the E693delta mutation has been developed. APP(OSK)-Tg mice exhibit intraneuronal Aβ E22delta oligomers and memory impairment as early as eight months of age.
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GA20096
(Des-Glu²²)-Amyloid β-Protein (1-42)
The Osaka (E22delta) mutation of Amyloid β promotes β-sheet transformation, radical production, and synaptotoxicity, but not neurotoxicity.
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GA20182
(Gln²²)-Amyloid β-Protein (1-40)
The Dutch mutation (E22Q) of amyloid β-peptide aggregates more readily than the wild-type peptide and the resulting fibrils show increased neurotoxicity. The mutant peptide E22Q induced apoptosis of cerebral endothelial cells at a concentration of 25 μm, whereas WT Aβ 1-40 and the Italian mutant E22K (H-6698) showed no effect.
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GA20183
(Gln²²)-Amyloid β-Protein (1-42)
The Dutch mutation (E22Q) aggregates more readily than the wild-type sequence. The resulting fibrils show increased neurotoxicity.
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GA20184
(Gln²²,Asn²³)-Amyloid β-Protein (1-40)
Transgenic mice expressing the vasculotropic Dutch/Iowa (E693Q/D694N) mutant human Aβ precursor protein in brain (Tg-SwDI) accumulate abundant cerebral microvascular fibrillar amyloid deposits and exhibit robust neuroinflammation. In vitro, the doubly mutated Aβ peptides showed an increased propensity to fibrillation and pathogenicity compared to the Dutch and Iowa single mutants.
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GA20181
(Gln¹¹)-Amyloid β-Protein (1-28)
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GA20186
(Gln⁹)-Amyloid β-Protein (1-40)
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GA20199
(Gly²²)-Amyloid β-Protein (1-40)
The highly neurotoxic arctic mutant (E22G) of Aβ has been used to study the mechanisms underlying the formation of soluble and insoluble β-amyloid aggregates. As the wild-type Aβ, the arctic mutant preferably assembles in the presence of GM1 ganglioside.
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GA20200
(Gly²²)-Amyloid β-Protein (1-42)
The arctic mutant of amyloid β peptide 1-42, in which Glu²² is substituted by Gly, is distinctly more amyloidogenic than the wild-type Aβ 1-42.
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GA20197
(Gly²¹)-Amyloid β-Protein (1-40)
Contrary to β-amyloid peptides mutated at position 22 (Dutch, Italian, Arctic mutants) the Flemish mutation (A21G) shows a decreased tendency to aggregate and a reduced neurotoxicity. In the studies of Betts and Tsubuki, A21G was degraded significantly more slowly by neprilysin than the wild-type Aβ 1-40 and the E22 mutants. The relative resistance to proteolytic degradation may account for the pathogenicity of the Aβ mutant.
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GA20198
(Gly²¹)-Amyloid β-Protein (1-42)
The Flemish mutation (A21G) shows a decreased tendency to aggregate and a reduced neurotoxicity. A21G is pathogenic as it is degraded significantly more slowly by neprilysin than WT Abeta42.
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GA20201
(Gly²⁸,Cys³⁰)-Amyloid β-Protein (1-30) amide
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GA20195
(Gly¹,Ser³·²²,Gln⁴·³⁴,Thr⁶,Arg¹⁹,Tyr²¹,Ala²³·³¹,Aib³²)-Pancreatic Polypeptide (human)
This (Ala-Aib)-containing pancreatic peptide/neuropeptide Y chimera is a highly selective neuropeptide Y? receptor agonist. At this receptor this compound turned out to be 25-fold more potent than the derivative H-5084 (0.24 nM vs 6 nM) and three-fold more potent than the native ligand neuropeptide Y (H-6375) (0.24 nM vs 0.6 nM). This analog turned out to increase feeding approximately 2.5-fold more effective than neuropeptide Y.
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GA20205
(H-Cys-Gly-OH)₂
NSC333711. Besides its reduced form, this product of glutathione metabolism is found in plasma.
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GA20221
(Hyp³)-Bradykinin
Bradykinin antagonist.
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GA20229
(Leu³¹,Pro³⁴)-Neuropeptide Y (human, rat)
Specific Y? receptor agonist.
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GA20244
(Lys²²)-Amyloid β-Protein (1-40)
The Italian mutation of β-amyloid 1-40 (E22K) aggregates more rapidly than the wild-type sequence 1-40. It showed increased neurotoxicity, which (according to a solid-phase NMR-study of Masuda et al.) may be due to the salt bridge formed between Lys²² and Asp²³ in the minor conformer. As the Arctic, Flemish, and Dutch mutants, the Italian mutant is degraded considerably more slowly than wild-type Aβ by neprilysin.
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GA20245
(Lys²²)-Amyloid β-Protein (1-42)
The Italian mutation (E22K) aggregates more rapidly than the wild-type sequence.
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GA20242
(Lys¹⁵)-Amyloid β-Protein (15-21)
KKLVFFA contains the KLVFF sequence, which is the minimum sequence binding the full-length amyloid β-protein. It showed improved water solubility compared with KLVFF (H-3682). It can be used as a labeled probe for screening defined sequences in the full-length amyloid β-protein.
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GA20251
(Met(O)³⁵)-Amyloid β-Protein (1-40)
Oxidation of Met35 attenuates the formation of Aβ40 oligomers.
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GA20252
(Met(O)³⁵)-Amyloid β-Protein (1-42)
(Met(O)³?)-Amyloid β-protein (1-42) (H-5888), in contrast to Aβ 1-42 (H-1368), has been shown to be non-toxic to 9-11 day-old rat embryonic hippocampal neuronal cultures and not to produce any protein oxidation. It has also been demonstrated that fibril formation is not affected by Met(O)³?. For the Nle analog see H-7308.
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GA20253
(Met(O)³⁵)-Amyloid β-Protein (25-35)
Sulfoxide of Aβ 25-35.
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GA20254
(Met(O₂)³⁵)-Amyloid β-Protein (1-42)
Maiti et al. could show that, in contrast to the sulfoxide of Aβ (1-42), the sulfone was as toxic and aggregated as fast as wild-type Aβ (1-42).
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GA20259
(Nle³⁵)-Amyloid β-Protein (1-40)
The reactive thioether of Met³? is crucial for the activity of Aβ 1-40 and Aβ 1-42. Due to the replacement of Met by inert Nle, M35Nle Aβ 1-40 was no longer toxic to cultured hippocampal neurons and had little effect on the level of protein carbonyl residues. The Nle peptide showed the same propensity to aggregate, whereas sulfoxide formation hindered the required conformational transition from random coil to β-sheet.
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GA20260
(Nle³⁵)-Amyloid β-Protein (1-42)
The thioether of Met³? plays a critical role in the oxidative stress induced by Aβ 1-42 and its neurotoxicity. The norleucine analog Aβ 1-42 M35Nle forms fibrils morphologically indistinguishable from the ones of the native sequence though lacking their neurotoxicity.
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GA20283
(Pyr³)-Amyloid β-Protein (3-40)
The pyroglutamate-modified amyloid-β peptides derived from Aβ40 (H-7422) and Aβ42 (H-4796) have gained considerable attention as potential key participants in the pathology of Alzheimer's disease (AD) due to their abundance in AD brain, high aggregation propensity, stability, and cellular toxicity. Aβ40 and 42 can be N-terminally truncated by action of cathepsin B. The cyclization of Glu³ is catalyzed by glutaminyl cyclase. Hence, inhibition of these enzymes could be a therapeutic approach to AD.
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GA20285
(Pyr³)-Amyloid β-Protein (3-42)
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GA20284
(Pyr³)-Amyloid β-Protein (3-42)
(Pyr³)-Amyloid β-Protein (3-42) was found to be the predominant amyloid β-peptide structure deposited in human brain of Alzheimer's disease and Down's syndrome patients. Therefore, (Pyr³)-Aβ (3-42) is suggested to accumulate in the brain and to trigger the formation of insoluble amyloid β-peptide deposits. Nussbaum et al. studies the Prion-like behaviour and tau-dependent cytotoxicity of the truncated Aβ sequence.
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GA20282
(Pyr¹¹)-Amyloid β-Protein (11-40)
pEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV, the N-terminally truncated isoform of the amyloid β-protein (Aβ) beginning with a pyroglutamate (Pyr) residue at position 11 was used in experiments studying the generality of fibrillogenesis-related helix formation. Comparing the fibrillogenesis kinetics of many of the most important clinically relevant amyloid β-protein alloforms it could be observed that among these peptides (Pyr¹¹)-amyloid β-protein (11-40) exhibited the greatest retardation of fibrillization rate.
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GA20291
(Sar¹)-Angiotensin II
The substitution with Sar at position 1 of angiotensin II resulted in a partial agonistic activity.
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GA20309
(Thr²)-Amyloid β-Protein (1-42)
A mutation very close to the β-secretase cleavage site of APP. The Icelandic mutation A2T of Aβ42 turned out to be less pathogenic than the native sequence. The precursor APP A673T was the first APP variant discovered in humans reducing the risk of Alzheimer's disease. A2T as well affects γ-secretase cleavage, the mutant was an inefficient substrate in a cell-based assay of the enzyme.
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GA20328
(Tyr¹¹)-Somatostatin-14
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GA20326
(Tyr¹)-Somatostatin-14