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Home >> Peptides

Peptides

Products for  Peptides

  1. Cat.No. Product Name Information
  2. GC62017 α-CGRP, rat TFA α-CGRP, rat TFA Chemical Structure
  3. GC62016 α-Conotoxin AuIB TFA α-Conotoxin AuIB TFA Chemical Structure
  4. GC38042 α-Factor Mating Pheromone, yeast (TFA) α-Factor Mating Pheromone, yeast (TFA) Chemical Structure
  5. GC63270 α-Glucosidase α-Glucosidase Chemical Structure
  6. GC63271 α-Synuclein (61-75) (TFA) α-Synuclein (61-75) (TFA) Chemical Structure
  7. GC38873 α2β1 Integrin Ligand Peptide TFA α2β1 Integrin Ligand Peptide TFA Chemical Structure
  8. GC37984 β-Amyloid (1-42), rat β-Amyloid (1-42), rat Chemical Structure
  9. GC61394 β-Amyloid (1-42), rat TFA β-Amyloid (1-42), rat TFA Chemical Structure
  10. GC61988 β-amyloid (12-28) (TFA) β-amyloid (12-28) (TFA) Chemical Structure
  11. GC39466 β-Amyloid 15-21 β-Amyloid 15-21 Chemical Structure
  12. GC37991 β-Amyloid 15-21 β-Amyloid 15-21 Chemical Structure
  13. GC38003 β-Casomorphin (1-5), bovine β-Casomorphin (1-5), bovine Chemical Structure
  14. GC60391 β-Casomorphin, bovine TFA β-Casomorphin, bovine TFA Chemical Structure
  15. GC61484 β-Casomorphin, human TFA β-Casomorphin, human TFA Chemical Structure
  16. GC34944 β-CGRP, human TFA β-CGRP, human TFA Chemical Structure
  17. 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. β-Defensin-3 (human) (trifluoroacetate salt) Chemical Structure
  18. 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. β-Defensin-4 (human) (trifluoroacetate salt) Chemical Structure
  19. 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). β-Endorphin (1-27) (human) (trifluoroacetate salt) Chemical Structure
  20. GC45236 β-Endorphin (rat) β-Endorphin (β-EP) is an endogenous opioid neuropeptide with diverse biological activities. β-Endorphin (rat) Chemical Structure
  21. GC38030 β-Endorphin, equine (TFA) β-Endorphin, equine (TFA) Chemical Structure
  22. GC38007 β-Melanocyte Stimulating Hormone (MSH), human TFA β-Melanocyte Stimulating Hormone (MSH), human TFA Chemical Structure
  23. GC61462 γ-1-Melanocyte Stimulating Hormone (MSH), amide γ-1-Melanocyte Stimulating Hormone (MSH), amide Chemical Structure
  24. GC62081 γ-Glu-Phe TFA γ-Glu-Phe TFA Chemical Structure
  25. GC17002 γ1-MSH melanocortin MC3 receptor agonist γ1-MSH Chemical Structure
  26. GC15513 ω-Agatoxin IVA P-type calcium channels blocker ω-Agatoxin IVA Chemical Structure
  27. GC12608 ω-Agatoxin TK CaV2.1 P/Q-type calcium channels blocker ω-Agatoxin TK Chemical Structure
  28. GC13886 ω-Conotoxin GVIA

    blocker of N-type calcium channels

     ω-Conotoxin GVIA Chemical Structure
  29. GC18070 ω-Conotoxin MVIIC wide spectrum blocker of N, P and Q type calcium channels ω-Conotoxin MVIIC Chemical Structure
  30. GC15519 α-CGRP (human)

    Endogenous calcitonin gene-related peptide receptor (CGRP) agonist

     α-CGRP (human) Chemical Structure
  31. GC10872 α-Conotoxin AuIB Selective antagonist of α3β4 nicotinic acetylcholine receptors α-Conotoxin AuIB Chemical Structure
  32. GC14296 α-Conotoxin PIA Selective antagonist of α6-containing nicotinic receptors α-Conotoxin PIA Chemical Structure
  33. GC10368 α-Conotoxin PnIA Selective antagonist of α3β2 nAChR receptors α-Conotoxin PnIA Chemical Structure
  34. GC30587 α-Factor Mating Pheromone, yeast (Mating Factor α) α-Factor Mating Pheromone, yeast (Mating Factor α) Chemical Structure
  35. GC11346 α-helical CRF 9-41 Antagonist of corticotropin releasing factor receptor α-helical CRF 9-41 Chemical Structure
  36. GC34242 β-Amyloid (1-42), rat TFA β-Amyloid (1-42), rat TFA Chemical Structure
  37. GC31146 β-Amyloid (10-35), amide β-Amyloid (10-35), amide Chemical Structure
  38. GC31129 β-Amyloid 1-16 (Amyloid β-Protein (1-16)) β-Amyloid 1-16 (Amyloid β-Protein (1-16)) Chemical Structure
  39. GC31171 β-Amyloid 1-28 (Amyloid β-Protein (1-28)) β-Amyloid 1-28 (Amyloid β-Protein (1-28)) Chemical Structure
  40. GC30325 β-Amyloid 22-35 (Amyloid β-Protein (22-35)) β-Amyloid 22-35 (Amyloid β-Protein (22-35)) Chemical Structure
  41. GC31137 β-Amyloid 29-40 (Amyloid beta-protein(29-40)) β-Amyloid 29-40 (Amyloid beta-protein(29-40)) Chemical Structure
  42. GC31179 β-Amyloid 31-35 β-Amyloid 31-35 Chemical Structure
  43. GC33736 β-Casomorphin, bovine (β-Casomorphin-7 (bovine)) β-Casomorphin, bovine (β-Casomorphin-7 (bovine)) Chemical Structure
  44. GC33784 β-Casomorphin, human (Human β-casomorphin 7) β-Casomorphin, human (Human β-casomorphin 7) Chemical Structure
  45. GC33585 β-catenin peptide β-catenin peptide Chemical Structure
  46. GC33595 β-CGRP, human (Human β-CGRP) β-CGRP, human (Human β-CGRP) Chemical Structure
  47. GC33693 β-Melanocyte Stimulating Hormone (MSH), human (Beta-MSH (1-22) (human)) β-Melanocyte Stimulating Hormone (MSH), human (Beta-MSH (1-22) (human)) Chemical Structure
  48. GC31172 δ-Sleep Inducing Peptide (Delta-Sleep Inducing Peptide) δ-Sleep Inducing Peptide (Delta-Sleep Inducing Peptide) Chemical Structure
  49. GC30187 γ-Glu-Phe (γ-Glutamylphenylalanine) γ-Glu-Phe (γ-Glutamylphenylalanine) Chemical Structure
  50. GC62067 ω-Conotoxin GVIA TFA ω-Conotoxin GVIA TFA Chemical Structure
  51. 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. ω-Conotoxin MVIIA Chemical Structure
  52. GC65232 (4R)-1-Boc-4-fluoro-D-proline (4R)-1-Boc-4-fluoro-D-proline Chemical Structure
  53. GC65484 (4S)-1-Boc-4-amino-D-proline (4S)-1-Boc-4-amino-D-proline Chemical Structure
  54. GC65235 (4S)-1-Boc-4-fluoro-D-proline (4S)-1-Boc-4-fluoro-D-proline Chemical Structure
  55. 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. (7-Diethylaminocoumarin-3-yl)carbonyl-Amyloid β-Protein (1-40) Chemical Structure
  56. 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. (Arg¹³)-Amyloid β-Protein (1-40) Chemical Structure
  57. GC34977 (Arg)9 TFA (Arg)9 TFA Chemical Structure
  58. 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. (Arg⁶)-Amyloid β-Protein (1-40) Chemical Structure
  59. 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. (Asn²³)-Amyloid β-Protein (1-40) Chemical Structure
  60. 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. (Asn⁶⁷⁰,Leu⁶⁷¹)-Amyloid β/A4 Protein Precursor₇₇₀ (667-675) Chemical Structure
  61. 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. (Asn⁶⁷⁰,Leu⁶⁷¹)-Amyloid β/A4 Protein Precursor₇₇₀ (667-676) Chemical Structure
  62. 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. (Asn⁶⁷⁰,Sta⁶⁷¹,Val⁶⁷²)-Amyloid β/A4 Protein Precursor₇₇₀ (662-675) Chemical Structure
  63. 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. (Asn⁷)-Amyloid β-Protein (1-40) Chemical Structure
  64. GA20045 (Asp³⁷)-Amyloid β-Protein (1-42) The G37D mutant does not show the aggregation behavior of WT Abeta42 nor its neurotoxicity. (Asp³⁷)-Amyloid β-Protein (1-42) Chemical Structure
  65. 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 (Cys²⁶)-Amyloid β-Protein (1-40) Chemical Structure
  66. GA20052 (Cys²⁶)-Amyloid β-Protein (1-40) (Dimer) Dimer of H-7402. (Cys²⁶)-Amyloid β-Protein (1-40) (Dimer) Chemical Structure
  67. 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. (Cys⁰)-Amyloid β-Protein (1-40) Chemical Structure
  68. GA20054 (Cys⁴⁷)-HIV-1 tat Protein (47-57) CPP for gene delivery. (Cys⁴⁷)-HIV-1 tat Protein (47-57) Chemical Structure
  69. 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. (D-Trp¹²,Tyr³⁴)-pTH (7-34) amide (bovine) Chemical Structure
  70. 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. (Des-Cys¹,cyclo(Ser²-Asu⁷))-Calcitonin (eel) Chemical Structure
  71. 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. (Des-Glu²²)-Amyloid β-Protein (1-40) Chemical Structure
  72. 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. (Des-Glu²²)-Amyloid β-Protein (1-42) Chemical Structure
  73. 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. (Gln²²)-Amyloid β-Protein (1-40) Chemical Structure
  74. 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. (Gln²²)-Amyloid β-Protein (1-42) Chemical Structure
  75. 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. (Gln²²,Asn²³)-Amyloid β-Protein (1-40) Chemical Structure
  76. GA20181 (Gln¹¹)-Amyloid β-Protein (1-28) (Gln¹¹)-Amyloid β-Protein (1-28) Chemical Structure
  77. GA20186 (Gln⁹)-Amyloid β-Protein (1-40) (Gln⁹)-Amyloid β-Protein (1-40) Chemical Structure
  78. 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. (Gly²²)-Amyloid β-Protein (1-40) Chemical Structure
  79. 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. (Gly²²)-Amyloid β-Protein (1-42) Chemical Structure
  80. 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. (Gly²¹)-Amyloid β-Protein (1-40) Chemical Structure
  81. 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. (Gly²¹)-Amyloid β-Protein (1-42) Chemical Structure
  82. GA20201 (Gly²⁸,Cys³⁰)-Amyloid β-Protein (1-30) amide (Gly²⁸,Cys³⁰)-Amyloid β-Protein (1-30) amide Chemical Structure
  83. 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. (Gly¹,Ser³·²²,Gln⁴·³⁴,Thr⁶,Arg¹⁹,Tyr²¹,Ala²³·³¹,Aib³²)-Pancreatic Polypeptide (human) Chemical Structure
  84. GA20205 (H-Cys-Gly-OH)₂ NSC333711. Besides its reduced form, this product of glutathione metabolism is found in plasma. (H-Cys-Gly-OH)₂ Chemical Structure
  85. GA20221 (Hyp³)-Bradykinin Bradykinin antagonist. (Hyp³)-Bradykinin Chemical Structure
  86. GA20229 (Leu³¹,Pro³⁴)-Neuropeptide Y (human, rat) Specific Y? receptor agonist. (Leu³¹,Pro³⁴)-Neuropeptide Y (human, rat) Chemical Structure
  87. 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. (Lys²²)-Amyloid β-Protein (1-40) Chemical Structure
  88. GA20245 (Lys²²)-Amyloid β-Protein (1-42) The Italian mutation (E22K) aggregates more rapidly than the wild-type sequence. (Lys²²)-Amyloid β-Protein (1-42) Chemical Structure
  89. 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. (Lys¹⁵)-Amyloid β-Protein (15-21) Chemical Structure
  90. GA20251 (Met(O)³⁵)-Amyloid β-Protein (1-40) Oxidation of Met35 attenuates the formation of Aβ40 oligomers. (Met(O)³⁵)-Amyloid β-Protein (1-40) Chemical Structure
  91. 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. (Met(O)³⁵)-Amyloid β-Protein (1-42) Chemical Structure
  92. GA20253 (Met(O)³⁵)-Amyloid β-Protein (25-35) Sulfoxide of Aβ 25-35. (Met(O)³⁵)-Amyloid β-Protein (25-35) Chemical Structure
  93. 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). (Met(O₂)³⁵)-Amyloid β-Protein (1-42) Chemical Structure
  94. 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. (Nle³⁵)-Amyloid β-Protein (1-40) Chemical Structure
  95. 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. (Nle³⁵)-Amyloid β-Protein (1-42) Chemical Structure
  96. 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. (Pyr³)-Amyloid β-Protein (3-40) Chemical Structure
  97. GA20285 (Pyr³)-Amyloid β-Protein (3-42) (Pyr³)-Amyloid β-Protein (3-42) Chemical Structure
  98. 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. (Pyr³)-Amyloid β-Protein (3-42) Chemical Structure
  99. 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. (Pyr¹¹)-Amyloid β-Protein (11-40) Chemical Structure
  100. GA20291 (Sar¹)-Angiotensin II The substitution with Sar at position 1 of angiotensin II resulted in a partial agonistic activity. (Sar¹)-Angiotensin II Chemical Structure
  101. 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. (Thr²)-Amyloid β-Protein (1-42) Chemical Structure

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