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Home >> Peptides

Peptides

Products for  Peptides

  1. Cat.No. Product Name Information
  2. GC66664 ((4-Chloro-3-(trifluoromethyl)phenyl)sulfonyl)valine ((4-Chloro-3-(trifluoromethyl)phenyl)sulfonyl)valine is a Valine derivative. ((4-Chloro-3-(trifluoromethyl)phenyl)sulfonyl)valine Chemical Structure
  3. GA24018 (2-(1,3-Dithiolan-2-yl)-Trp²?)-Liraglutide trifluoroacetate salt The peptide is an impurity of Liraglutide. (2-(1,3-Dithiolan-2-yl)-Trp²?)-Liraglutide trifluoroacetate salt Chemical Structure
  4. GA24019 (2-(2-Trifluoromethyl-1,3-dithiolan-2-yl)-Trp²?)-Liraglutide trifluoroacetate salt The peptide is an impurity of Liraglutide. (2-(2-Trifluoromethyl-1,3-dithiolan-2-yl)-Trp²?)-Liraglutide trifluoroacetate salt Chemical Structure
  5. GA24020 (2-Hydroxy-Trp²?)-Liraglutide trifluoroacetate salt The peptide is an impurity of Liraglutide. (2-Hydroxy-Trp²?)-Liraglutide trifluoroacetate salt Chemical Structure
  6. GC68059 (2R,2'R)-4,4'-Disulfanediylbis(2-aminobutanoic acid) (2R,2'R)-4,4'-Disulfanediylbis(2-aminobutanoic acid) Chemical Structure
  7. GC68248 (2R,3S)-3-Phenylisoserine hydrochloride

    Benzenepropanoic acid, β-amino-α-hydroxy-, hydrochloride, (αR,βS)-

     (2R,3S)-3-Phenylisoserine hydrochloride Chemical Structure
  8. GC66180 (2S)-2-[(tert-Butoxycarbonyl)amino]-3-(3,4-difluorophenyl)propionic acid (2S)-2-[(tert-Butoxycarbonyl)amino]-3-(3,4-difluorophenyl)propionic acid is a phenylalanine derivative. (2S)-2-[(tert-Butoxycarbonyl)amino]-3-(3,4-difluorophenyl)propionic acid Chemical Structure
  9. GC68261 (2S)-2-[(tert-Butoxycarbonyl)amino]-3-(3-fluorophenyl)propionic acid

    (S)-2-[(tert-Butoxycarbonyl)amino]-3-(3-fluorophenyl)propionic acid; tert-Butoxycarbonyl-L-3-fluorophenylalanine

     (2S)-2-[(tert-Butoxycarbonyl)amino]-3-(3-fluorophenyl)propionic acid Chemical Structure
  10. GC68251 (2S)-4-(benzyloxy)-2-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-4-oxobutanoic acid (2S)-4-(benzyloxy)-2-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-4-oxobutanoic acid Chemical Structure
  11. GC68224 (2S)-Methyl 2-(2-cyclohexyl-2-(pyrazine-2-carboxamido)acetamido)-3,3-dimethylbutanoate (2S)-Methyl 2-(2-cyclohexyl-2-(pyrazine-2-carboxamido)acetamido)-3,3-dimethylbutanoate Chemical Structure
  12. GC68083 (2S,3R)-Ethyl 2-amino-3-hydroxybutanoate hydrochloride (2S,3R)-Ethyl 2-amino-3-hydroxybutanoate hydrochloride Chemical Structure
  13. GC68238 (2S,4R)-1-((9H-Fluoren-9-yl)methyl) 2-methyl 4-hydroxypyrrolidine-1,2-dicarboxylate (2S,4R)-1-((9H-Fluoren-9-yl)methyl) 2-methyl 4-hydroxypyrrolidine-1,2-dicarboxylate Chemical Structure
  14. GC68225 (2S,4R)-1-((S)-2-((tert-butoxycarbonyl)amino)non-8-enoyl)-4-hydroxypyrrolidine-2-carboxylic acid (2S,4R)-1-((S)-2-((tert-butoxycarbonyl)amino)non-8-enoyl)-4-hydroxypyrrolidine-2-carboxylic acid Chemical Structure
  15. GC67811 (2S,4R)-4-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-1-(tert-butoxycarbonyl)pyrrolidine-2-carboxylic acid (2S,4R)-4-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-1-(tert-butoxycarbonyl)pyrrolidine-2-carboxylic acid Chemical Structure
  16. GC68105 (3-Aminopropyl)glycine (3-Aminopropyl)glycine Chemical Structure
  17. GC68128 (3R,4R)-4-(benzyloxy)-3-((tert-butoxycarbonyl)amino)pentanoic acid (3R,4R)-4-(benzyloxy)-3-((tert-butoxycarbonyl)amino)pentanoic acid Chemical Structure
  18. GC67959 (3S,4R,5S)-rel-3-(3-Chloro-2-fluorophenyl)-4-(4-chloro-2-fluorophenyl)-4-cyano-5-neopentylpyrrolidine-2-carboxylic acid (3S,4R,5S)-rel-3-(3-Chloro-2-fluorophenyl)-4-(4-chloro-2-fluorophenyl)-4-cyano-5-neopentylpyrrolidine-2-carboxylic acid Chemical Structure
  19. GC65232 (4R)-1-Boc-4-fluoro-D-proline (4R)-1-Boc-4-fluoro-D-proline is an amino acid derivative that can be used for preparation of peptidomimetics, dihydropyridopyrimidines and pyridopyrimidines. (4R)-1-Boc-4-fluoro-D-proline Chemical Structure
  20. GC66649 (4R)-2,2-Dimethyl-4-thiazolidinecarboxylic Acid (4R)-2,2-Dimethyl-4-thiazolidinecarboxylic Acid is a cysteine derivative. (4R)-2,2-Dimethyl-4-thiazolidinecarboxylic Acid Chemical Structure
  21. GC65484 (4S)-1-Boc-4-amino-D-proline (4S)-1-Boc-4-amino-D-proline is an amino acid derivative that can be used for compound synthesis. (4S)-1-Boc-4-amino-D-proline Chemical Structure
  22. GC65235 (4S)-1-Boc-4-fluoro-D-proline (4S)-1-Boc-4-fluoro-D-proline is a derivative of fluoro-D-proline, can be used for synthesis of compounds. (4S)-1-Boc-4-fluoro-D-proline Chemical Structure
  23. GC68190 (6S,9S,12S)-Benzyl 12-benzyl-9-isobutyl-2,2-dimethyl-4,7,10-trioxo-6-phenethyl-3-oxa-5,8,11-triazatridecan-13-oate (6S,9S,12S)-Benzyl 12-benzyl-9-isobutyl-2,2-dimethyl-4,7,10-trioxo-6-phenethyl-3-oxa-5,8,11-triazatridecan-13-oate Chemical Structure
  24. 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
  25. GA24022 (Ala¹³)-Apelin-13 (human, bovine, mouse, rat) (Salt form acetate)

    (Ala13)-Apelin 13, human

     (Ala13)-Apelin 13 showed scavenging abilities against active oxygen species such as superoxide and hydroxyl radicals. (Ala¹³)-Apelin-13 (human, bovine, mouse, rat) (Salt form acetate) Chemical Structure
  26. GA24023 (Ala¹³)-Apelin-13 (human, bovine, mouse, rat) (Salt form trifluoroacetate) Specific anatagonist of apelin-13. (Ala¹³)-Apelin-13 (human, bovine, mouse, rat) (Salt form trifluoroacetate) Chemical Structure
  27. GA24021 (Ala¹)-PAR-4 (1-6) (mouse)

    (Ala¹)-Thrombin Receptor-Like 3 (1-6) (mouse)

     (Ala¹)-PAR-4 (1-6) (mouse) Chemical Structure
  28. GC41696 (Ala1)-PAR4 (1-6) (mouse) (trifluoroacetate salt)

    H-Ala-Tyr-Pro-Gly-Lys-Phe-OH, AYPGKF

     (Ala1)-PAR4 (1-6) is a synthetic peptide agonist of proteinase-activated receptor 4 (PAR4) that corresponds to residues 1-6 of the amino terminal tethered ligand sequence of mouse PAR4 and residues 60-65 of the full-length sequence with an alanine residue substituted for glycine at position 1/60. (Ala1)-PAR4 (1-6) (mouse) (trifluoroacetate salt) Chemical Structure
  29. GC41697 (Ala1)-PAR4 (1-6) amide (mouse) (trifluoroacetate salt)

    AY-NH2, AYPGKF-NH2, H-Ala-Tyr-Pro-Gly-Lys-Phe-NH2, PAR4-AP, Proteinase-Activated Receptor 4 Activating Peptide

     (Ala1)-PAR4 (1-6) amide (mouse) is a peptide agonist of proteinase-activated receptor 4 (PAR4) that induces aggregation of rat and human platelets in vitro (EC50s = 15 and 60 μM, respectively). (Ala1)-PAR4 (1-6) amide (mouse) (trifluoroacetate salt) Chemical Structure
  30. 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
  31. GC66389 (Arg)9 acetate

    Nona-L-arginine acetate; Peptide R9 acetate

     (Arg)9 (Nona-L-arginine) acetate is a cell-penetrating peptide (CPP) made up of 9 arginine residues. (Arg)9 acetate has neuroprotective property, exhibits neuroprotective activity with an IC50 of 0.78 μM in the glutamic acid model. (Arg)9 acetate Chemical Structure
  32. GC34977 (Arg)9 TFA

    Nona-L-arginine TFA; Peptide R9 TFA

     (Arg)9 TFA (Nona-L-arginine TFA), a cell-penetrating peptide, exhibits neuroprotective activity with an IC50 of 0.78 μM in the glutamic acid model. (Arg)9 TFA Chemical Structure
  33. GC68684 (Arg)9, FAM-labeled

    (Arg)9, labeled with FAM, is a cell-penetrating peptide (CPP) that has been tagged with the fluorescent dye FAM. CPPs have become powerful tools for delivering bioactive substances into intact cell cytoplasm.

     (Arg)9, FAM-labeled Chemical Structure
  34. 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
  35. 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
  36. 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
  37. 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
  38. 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
  39. 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
  40. GA24025 (Aspartimide²¹)-Glucagon trifluoroacetate salt The peptide is an impurity of glucagon. (Aspartimide²¹)-Glucagon trifluoroacetate salt Chemical Structure
  41. GA24024 (Aspartimide¹?)-Glucagon trifluoroacetate salt The peptide is an impurity of glucagon. (Aspartimide¹?)-Glucagon trifluoroacetate salt Chemical Structure
  42. 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
  43. GC68109 (Cyclohexanecarbonyl)-L-leucine (Cyclohexanecarbonyl)-L-leucine Chemical Structure
  44. GA24026 (Cys(S)²)-Octreotide Potential impurity of octreotide. (Cys(S)²)-Octreotide Chemical Structure
  45. GA24027 (Cysteinol?,des-L-threoninol?)-Octreotide Impuritiy of octreotide. (Cysteinol?,des-L-threoninol?)-Octreotide Chemical Structure
  46. 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
  47. GA20052 (Cys²⁶)-Amyloid β-Protein (1-40) (Dimer) Dimer of H-7402. (Cys²⁶)-Amyloid β-Protein (1-40) (Dimer) Chemical Structure
  48. 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
  49. GA20054 (Cys⁴⁷)-HIV-1 tat Protein (47-57) (Cys⁴⁷)-HIV-1 tat Protein (47-57) has membrane translocation function and can be used to derivatize the surface of magnetic pharmaceuticals and substantially facilitated their uptake into target cells. (Cys⁴⁷)-HIV-1 tat Protein (47-57) Chemical Structure
  50. GA24028 (d(CH?)?¹,D-Ile²,Ile?,Arg?,Tyr?)-Vasopressin

    d(CH2)5[D-Ile2,Ile4,Tyr9]-AVP

     AVP antagonist specifically targeting the rat V2 receptor. (d(CH?)?¹,D-Ile²,Ile?,Arg?,Tyr?)-Vasopressin Chemical Structure
  51. GA24029 (d(CH?)?¹,Tyr(Me)²,Dab?,Arg?)-Vasopressin

    d(CH2)5[Tyr(Me)2,Dab5]-AVP

     The isosteric substitution of Asn5 by Dab in oxytocin, vasopressin and their analogs invariably leads to a dramatic loss of the biolical activities of the peptides. (d(CH?)?¹,Tyr(Me)²,Dab?,Arg?)-Vasopressin Chemical Structure
  52. GA24030 (d(CH?)?¹,Tyr(Me)²,Dab?,Arg?,Tyr?)-Vasopressin

    d(CH2)5[Tyr(Me)2,Dab5]-AVP

     Replacement of Asn5 by isosteric Dab generates a vasopressin antagonist. (d(CH?)?¹,Tyr(Me)²,Dab?,Arg?,Tyr?)-Vasopressin Chemical Structure
  53. GA24031 (D-Ala¹?)-Liraglutide trifluoroacetate salt The peptide is an impurity of Liraglutide. (D-Ala¹?)-Liraglutide trifluoroacetate salt Chemical Structure
  54. GA24032 (D-Arg?)-Inotocin

    [D-Arg8]-Inotocin

     Analog of the insect neuropeptide inotocin acting as human vasopressin V1a-receptor antagonist. (D-Arg?)-Inotocin Chemical Structure
  55. GA24033 (D-Cys?,des-L-threoninol?)-Octreotide Potential impurity of octreotide. (D-Cys?,des-L-threoninol?)-Octreotide Chemical Structure
  56. GA24034 (Deamino-Cys¹)-Oxytocin

    dOT

     Oxytocin analog with prolonged activity. (Deamino-Cys¹)-Oxytocin Chemical Structure
  57. GA24038 (Deamino-Cys¹,β-cyclohexyl-Ala?,Dab?)-Vasopressin

    d[Cha4,Dab8]-AVP

     Introduction of Cha generates agonists for the human V1b receptor. (Deamino-Cys¹,β-cyclohexyl-Ala?,Dab?)-Vasopressin Chemical Structure
  58. GA24035 (Deamino-Cys¹,Arg?)-Vasopressin

    dAVP

     (Deamino-Cys¹,Arg?)-Vasopressin is a used to treat diabetes insipidus, bedwetting, hemophilia A, von Willebrand disease, and high blood urea levels. (Deamino-Cys¹,Arg?)-Vasopressin Chemical Structure
  59. GA24036 (Deamino-Cys¹,Lys?)-Oxytocin

    dOTK8

     Desamino-LVT showed the oxytocic activity of Lysine-vasotocin without detectable pressor activity. (Deamino-Cys¹,Lys?)-Oxytocin Chemical Structure
  60. GA24037 (Deamino-Cys¹,Tyr(Me)²,Val?,D-Arg?)-Vasopressin

    d[Tyr(Me2)]VdAVP

     A highly specific and potent antidiuretic AVP agonist. (Deamino-Cys¹,Tyr(Me)²,Val?,D-Arg?)-Vasopressin Chemical Structure
  61. 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
  62. 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
  63. 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
  64. GA24039 (Des-Gly²?)-Liraglutide trifluoroacetate salt The peptide is an impurity of Liraglutide. (Des-Gly²?)-Liraglutide trifluoroacetate salt Chemical Structure
  65. GA24040 (Des-Gly³¹)-Liraglutide trifluoroacetate salt The peptide is an impurity of Liraglutide. (Des-Gly³¹)-Liraglutide trifluoroacetate salt Chemical Structure
  66. GA24041 (Des-His¹)-Glucagon trifluoroacetate salt

    Glucagon (2-29)

     The peptide is an impurity of glucagon. (Des-His¹)-Glucagon trifluoroacetate salt Chemical Structure
  67. GA24042 (Des-L-threoninol?)-Octreotide amide Potential impurity of octreotide. (Des-L-threoninol?)-Octreotide amide Chemical Structure
  68. GC41699 (Des-octanoyl)-Ghrelin (human) (trifluoroacetate salt) Ghrelin is an endogenous gastrointestinal hormone and neuropeptide that binds to the growth hormone (GH) secretagogue receptor (GHS-R). (Des-octanoyl)-Ghrelin (human) (trifluoroacetate salt) Chemical Structure
  69. GA24043 (Des-Ser?)-Liraglutide trifluoroacetate salt The peptide is an impurity of Liraglutide. (Des-Ser?)-Liraglutide trifluoroacetate salt Chemical Structure
  70. 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
  71. 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
  72. 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
  73. GA20181 (Gln¹¹)-Amyloid β-Protein (1-28) (Gln¹¹)-Amyloid β-Protein (1-28) Chemical Structure
  74. GA20186 (Gln⁹)-Amyloid β-Protein (1-40) (Gln⁹)-Amyloid β-Protein (1-40) Chemical Structure
  75. 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
  76. 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
  77. 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
  78. 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
  79. GA24046 (Gly?,Thr?,Ser?)-Oxytocin

    kB7-OT

     The cyclopeptide kB7-OT1 was designed using the kalata B7 loop 3 as template. (Gly?,Thr?,Ser?)-Oxytocin Chemical Structure
  80. GA20201 (Gly²⁸,Cys³⁰)-Amyloid β-Protein (1-30) amide (Gly²⁸,Cys³⁰)-Amyloid β-Protein (1-30) amide Chemical Structure
  81. GA20195 (Gly¹,Ser³·²²,Gln⁴·³⁴,Thr⁶,Arg¹⁹,Tyr²¹,Ala²³·³¹,Aib³²)-Pancreatic Polypeptide (human) (Gly¹,Ser³.²²,Gln⁴.³⁴,Thr⁶,Arg¹⁹,Tyr²¹,Ala²³.³¹,Aib³²)-Pancreatic Polypeptide (human) is a potent and selective neuropeptide Y Y5 receptor agonist with an IC50 of 0.24 nM for binding to the hY5 receptor. (Gly¹,Ser³·²²,Gln⁴·³⁴,Thr⁶,Arg¹⁹,Tyr²¹,Ala²³·³¹,Aib³²)-Pancreatic Polypeptide (human) Chemical Structure
  82. GA20205 (H-Cys-Gly-OH)₂

    (Cys-Gly)2, (H-Cys-Gly-OH)2, NSC 333711

     NSC333711. Besides its reduced form, this product of glutathione metabolism is found in plasma. (H-Cys-Gly-OH)₂ Chemical Structure
  83. GA20221 (Hyp³)-Bradykinin (Hyp³)-Bradykinin, naturally occurring peptide hormone, is a bradykinin receptor agonist. (Hyp³)-Bradykinin Chemical Structure
  84. GA24047 (Kyn²?)-Liraglutide trifluoroacetate salt The peptide is an impurity of Liraglutide. (Kyn²?)-Liraglutide trifluoroacetate salt Chemical Structure
  85. GA24049 (L-Threoninol(Ac)?)-Octreotide Potential impurity of octreotide. (L-Threoninol(Ac)?)-Octreotide Chemical Structure
  86. GA24048 (Leu¹³)-Motilin (human, porcine) (Leu¹³)-Motilin (human, porcine) has been shown to produce an excitory response in the chicken gastrointestinal tract with a different sensitivity from region to region. (Leu¹³)-Motilin (human, porcine) Chemical Structure
  87. GA20229 (Leu³¹,Pro³⁴)-Neuropeptide Y (human, rat) (Leu³¹,Pro³⁴)-Neuropeptide Y (human, rat) is a specific neuropeptide Y Y1 receptor agonist. (Leu³¹,Pro³⁴)-Neuropeptide Y (human, rat) Chemical Structure
  88. 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
  89. 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
  90. GA24050 (Lys(Ac)?)-Octreotide Potential impurity of octreotide. (Lys(Ac)?)-Octreotide Chemical Structure
  91. 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
  92. 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
  93. 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
  94. GA20253 (Met(O)³⁵)-Amyloid β-Protein (25-35) Sulfoxide of Aβ 25-35. (Met(O)³⁵)-Amyloid β-Protein (25-35) Chemical Structure
  95. 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
  96. 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
  97. 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
  98. GA24051 (Pro?)-Oxytocin

    (Pro?)-Vasotocin

     The L8P variant of oxytocin is produced by the Cebidae family of New World monkeys. (Pro?)-Oxytocin Chemical Structure
  99. 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
  100. 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
  101. 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

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