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≥95% (HPLC)

L-Seryl-L-asparaginyl-L-tryptophyl-L-lysyl-L-tryptophyl-L-tryptophyl-L-prolylglycyl-L-isoleucyl-L-phenylalanyl-L-aspartic acid trifluoroacetate salt
Empirical Formula (Hill Notation):
C72H90N16O16 · xC2HF3O2
Molecular Weight:
1435.58 (free base basis)
PubChem Substance ID:

Quality Level


≥95% (HPLC)


white powder


H2O: >1 mg/mL

storage temp.


SMILES string




InChI key



QBP1, an oligopeptide inhibitor of polyglutamine protein aggregation, may be used to study the physicochemical processes of polyglutamine-dependent protein misfolding, aggregation and precipitation. QBP1 may be used to study the role polyglutamine protein aggregation in causing or aggravating polyglutamine diseases including neurodegenerative diseases such as Huntington′s dentatorubral pallidoluysian atrophy, spinobulbar muscular atrophy, and spinocerebellar ataxia.


1 mg in glass bottle

Biochem/physiol Actions

QBP1 is an inhibitor of polyglutamine protein aggregation and cell death. QBP1 inhibits polyglutamine aggregation in COS-7 cells at a concentration of 25 μM, as shown by complete inhibition of thioredoxin-Q62 aggregation assayed by turbidity at 405 nm. QBP1 reduces cell death of these cells by 50% and increases median life span from 5.5-52 days in Drosophilla melanogaster that expresses the expanded polyglutamine; can be shortened to 8 amino acids (Trp-Ley-Trp-Trp-Pro-Gly-Ile-Phe) without the loss of ability to inhibit polyglutamine aggregation. Several inherited neurodegenerative diseases, Huntington′s dentatorubral pallidoluysian atrophy, spinobulbar muscular atrophy, and spinocerebellar ataxia are caused by the expanded CAG repeats in the coding region of the gene, leading to accumulation of polyglutamine.

Storage Class Code

11 - Combustible Solids

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

Miguel Mompeán et al.
Archives of biochemistry and biophysics, 675, 108113-108113 (2019-10-01)
Transactive Response DNA-Binding Protein of 43 kDa (TDP-43) is an essential human protein implicated in Amyotrophic Lateral Sclerosis (ALS) and common dementias. Its C-terminal disordered region, composed of residues 264-414 includes a hydrophobic segment (residues 320-340), which drives physiological liquid/liquid phase...
Amit Mishra et al.
The Journal of biological chemistry, 283(12), 7648-7656 (2008-01-19)
The accumulation of intracellular protein deposits as inclusion bodies is the common pathological hallmark of most age-related neurodegenerative disorders including polyglutamine diseases. Appearance of aggregates of the misfolded mutant disease proteins suggest that cells are unable to efficiently degrade them...
Peter O Bauer et al.
Nature biotechnology, 28(3), 256-263 (2010-03-02)
Huntington's Disease (HD) is a dominantly inherited pathology caused by the accumulation of mutant huntingtin protein (HTT) containing an expanded polyglutamine (polyQ) tract. As the polyglutamine binding peptide 1 (QBP1) is known to bind an expanded polyQ tract but not...
H Akiko Popiel et al.
PloS one, 7(11), e51069-e51069 (2012-12-12)
The polyglutamine (polyQ) diseases such as Huntington's disease (HD), are neurodegenerative diseases caused by proteins with an expanded polyQ stretch, which misfold and aggregate, and eventually accumulate as inclusion bodies within neurons. Molecules that inhibit polyQ protein misfolding/aggregation, such as...

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