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[Ala8] - Humanin, [Ala8] - HN, Shna

Protection activity of humanin (HN) against neuronal cell death is abrogated in this peptide, where Cys8 is substituted by Ala.

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[alpha]-Bag Cell Peptide (1 - 7) ( APRLRFY )

The heptapeptide APRLRFY from Aplysia parvula acts as a neurotransmitter locally, upon neurons of the abdominal ganglion and as a hormone by diffusing into the circulating hemolymph and modulating the activity of other organs. It specifically causes contraction of smooth muscle in the ovotestis and expulsion of the egg string.

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[alpha]-Bag Cell Peptide (1 - 8) ( APRLRFYS )

The octapeptide APRLRFYS from Aplysia parvula acts as a neurotransmitter locally, upon neurons of the abdominal ganglion and as a hormone by diffusing into the circulating hemolymph and modulating the activity of other organs. It specifically causes contraction of smooth muscle in the ovotestis and expulsion of the egg string.

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[alpha]-Bag Cell Peptide (1 - 9) ( APRLRFYSL )

The nonapeptide APRLRFYSL from Aplysia parvula acts as a neurotransmitter locally, upon neurons of the abdominal ganglion and as a hormone by diffusing into the circulating hemolymph and modulating the activity of other organs. It specifically causes contraction of smooth muscle in the ovotestis and expulsion of the egg string.

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[alpha]-Casein (90-95) ( RYLGYL )

bioactive peptide

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[beta]-Amyloid (1-14)

Beta-amyloid peptide (Abeta), the major constituent of amyloid plaques in the brains of Alzheimer’s patients, is thought to be the cause of Alzheimer’s Disease (AD). AD is the most common neurodegenerative disease and afflicts about 10% of the population over 60.

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[beta]-Amyloid (1-15)

Aβ (1-15) was used in a study investigating the presence of conformational epitope/s (mimotope/s) on fibrillar amyloid β-protein (1-42). The N-terminal Aβ fragments Aβ1-14, Aβ1-15, and Aβ1-16 are elevated in cell media and in CSF in response to γ-secretase inhibitor treatment. The fragments can serve as biomarkers in clinical studies of the effect of such inhibitors.

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[beta]-Amyloid (1-16)

The Cu²⁺ complex of this soluble amyloid β-protein fragment showed significant oxidative activities toward the catechol-like substrate 1,2,3-trihydroxylbenzene (pyrogallol) and plasmid DNA cleavage. The N-terminal Aβ fragments Aβ1-14, Aβ1-15, and Aβ1-16 are elevated in cell media and in CSF in response to γ-secretase inhibitor treatment. The fragments can serve as biomarkers in clinical studies of the effect of such inhibitors. Proteins interactions with reactive oxygen agents may result in covalent modifications of amino acid residues in proteins, formation of protein-protein cross-linkages and oxidation of the protein backbone resulting in protein fragmentation. Oxidation targets for Aß(1-16) are the histidine residues coordinated to the metal ions. Copper is bound to Aß in senile plaque of Alzheimer’s disease with Aß (1-16) taking part in the coordination of the Cu2+ ions. Cu2+ and Zn2+ are linked with the neurotoxicity of Aß and free radical damage.

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[beta]-Amyloid (1-28)

The three-dimensional solution structure of Aß (1-28) reveals the folding of the peptide to form a predominantly a-helical structure with a bend centered at residue 12 and the side chains of histidine-13 and lysine-16 in close proximity, residing on the same face of the helix. Their proximity may constitute a binding motif with the heparan sulfate proteoglycans. Aß (1-28) is highly hydrophilic and shares sequences with bA4, the major component of Aß. Its assembly is fibrillar, i.e., elongated in a single direction. Reports show that synthetic peptides Aß (1-40) and Aß (1-28) have significant effects on normal human plasma cholesterol esterification rate. Both peptides (at concentration of 1 ng/mL) inhibit plasma cholesterol esterification rate by 40-50% compared to the control value.

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[beta]-Amyloid (1-39)

A number of Aß protein variants, differing only at their carboxy terminus (1-39, 1-40, 1-42 and 1-43), are identified as the major components of the cerebral amyloid deposits in Alzheimer’s disease. The length of the C-terminus is a critical determinant of the rate of amyloid formation (“kinetic solubility”), with only a minor effect on the thermodynamic solubility. Amyloid formation by the kinetically soluble peptides (e.g. 1-39) can be nucleated, or “seeded” by peptides which include the critical C-terminal residues (1-42, 26-42, 26-43, 34-42).

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[beta]-Amyloid (1-40), rat

A number of Aß protein variants, differing only at their carboxy terminus (1-39, 1-40, 1-42 and 1-43), are identified as the major components of the cerebral amyloid deposits in Alzheimer’s disease. The length of the C-terminus is a critical determinant of the rate of amyloid formation (“kinetic solubility”), with only a minor effect on the thermodynamic solubility. Amyloid formation by the kinetically soluble peptides (e.g. 1-40) can be nucleated, or “seeded” by peptides which include the critical C-terminal residues (1-42, 26-42, 26-43, 34-42).

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[beta]-Amyloid (10-35)

Amyloid β-protein (10-35), YEVHHQKLVFFAEDVGSNKGAIIGLM, was used as a truncated peptide model for the full-length amyloid β-proteins (1-40) and (1-42) in high-resolution structural studies. In contrast to the full-length amyloid β-proteins, amyloid β-protein (10-35) allowed the controlled and reproducible formation of homogeneous fibrils from aqueous solutions of defined pH, ionic strength and soluble peptide concentration necessary for high-resolution structural studies.

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[beta]-Amyloid (12-28)

Aβ (12-28) represents a binding site for apolipoprotein E (apoE). ApoE is a genetically inherited risk factor for Alzheimer’s disease that promotes aggregation of toxic Aβ. This sequence encompasses a hydrophobic domain (residues 14–21) and a ß-turn (residues 22–28) which place two hydrophobic domains of Aß 14 to 21 and 29 to 40/42 opposite each other, allowing for the assembly of Aß peptides into fibrils. The secondary structure of Aß (12- 28), a neutral peptide, is dominated by a-helix and random coil. The interaction of apoE with residues 12 to 28 of Aß is not just a non-specific hydrophobic interaction but plays a pivotal role in the mechanism of Aß pathology in Alzheimer’s disease (AD). Aß (11-28) and five other fragments enhanced aggregation of full length Aß (1-40). All of the peptides that enhance aggregation contained either residues 17 to 20 or 30 to 35, indicating the importance of these regions for promoting aggregation of full-length Aß.

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[beta]-Amyloid (13-27)

This β-Amyloid peptide 13 to 27 amino acid residues was used to study the kinetics of β-amyloid formation.

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[beta]-Amyloid (16-23) ( KLVFFAED )

This octapeptide beta-Amyloid 16 to 23 was used in exploring the design of potential inhibitors of amyloidogenesis. This peptide is capable of forming thin flakes, while the shortest fibril-forming sequence was found to be the decapeptide b-Amyloid 14 to 23.

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[beta]-Amyloid (22-35)

Aβ (22-35), EDVGSNKGAIIGLM, forms amyloid fibrils in vitro resembling those of the β-amyloid protein in senile plaques and exhibits a toxicity profile that parallels that of full-length Aβ (1-40) and Aβ (1-42) in hippocampal and cortical neurons in cell culture.

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[beta]-Casomorphin (1-7), bovine ( YPFPGPI )

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[Phe17] - Apelin

Apelin has been found to be expressed in the spinal cord and the human brain and when performing immunohistochemistry it was observed that apelin-17 is significantly expressed in the human heart, brain, lungs and endothelial cells.

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3x FLAG Peptide

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AAV VP1 492-500 (HLA-A*01:01) ( SADNNNSEY )

AAV VP1 492-500 with the amino acid sequence SADNNNSEY is a peptidic epitope (epitope ID 189272) that is studied as part of two proteins: Capsid protein VP1 (UniProt:P03135) from Dependoparvovirus primate1 (Adeno-associated dependoparvovirus A) and Capsid protein (UniProt:A0A1C8Z4Q6) from Adeno-associated virus.

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ABI2 145-153 (HLA-A*02:01) ( ILDDIGHGV )

control peptide

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ABL1 (HLA-A*02:01) ( CLWCVPQLR )

This gene is a protooncogene that encodes a protein tyrosine kinase involved in a variety of cellular processes, including cell division, adhesion, differentiation, and response to stress. The activity of the protein is negatively regulated by its SH3 domain, whereby deletion of the region encoding this domain results in an oncogene. The ubiquitously expressed protein has DNA-binding activity that is regulated by CDC2-mediated phosphorylation, suggesting a cell cycle function. This gene has been found fused to a variety of translocation partner genes in various leukemias, most notably the t(9;22) translocation that results in a fusion with the 5' end of the breakpoint cluster region gene (BCR; MIM:151410). Alternative splicing of this gene results in two transcript variants, which contain alternative first exons that are spliced to the remaining common exons.

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ACTH (1-10), human ( SYSMEHFRWG )

Adrenocorticotropic hormone (ACTH), also known as corticotropin, is produced and secreted by the anterior pituitary gland. ACTH is an important component of the hypothalamic-pituitary-adrenal axis as a response to biological stress.ACTH (1-10), human with the amino acid sequence SYSMEHFRWG is a synthetic peptide corresponding to the first 10 amino acids of human ACTH.

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ACTH (1-39), human

ACTH (1-39), human is a synthetic peptide corresponding to the first 39 amino acids of human ACTH/adrenocorticotropin which is the major regulator of adrenal cortex function. ACTH stimulates the synthesis of steroidal hormones.

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