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Merck

Q4990

Sigma-Aldrich

QBP1

≥95% (HPLC)

Synonim(y):

L-Seryl-L-asparaginyl-L-tryptophyl-L-lysyl-L-tryptophyl-L-tryptophyl-L-prolylglycyl-L-isoleucyl-L-phenylalanyl-L-aspartic acid trifluoroacetate salt

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About This Item

Wzór empiryczny (zapis Hilla):
C72H90N16O16 · xC2HF3O2
Numer CAS:
Masa cząsteczkowa:
1435.58 (free base basis)
Kod UNSPSC:
12352203
Identyfikator substancji w PubChem:
NACRES:
NA.25

Próba

≥95% (HPLC)

Postać

powder

kolor

white

rozpuszczalność

H2O: >1 mg/mL

temp. przechowywania

−20°C

ciąg SMILES

OC(=O)C(F)(F)F.CC[C@H](C)[C@H](NC(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@H](Cc2c[nH]c3ccccc23)NC(=O)[C@H](Cc4c[nH]c5ccccc45)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc6c[nH]c7ccccc67)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](N)CO)C(=O)N[C@@H](Cc8ccccc8)C(=O)N[C@@H](CC(O)=O)C(O)=O

InChI

1S/C72H90N16O16.C2HF3O2/c1-3-39(2)62(70(101)84-52(28-40-16-5-4-6-17-40)65(96)86-57(72(103)104)33-61(92)93)87-60(91)37-79-69(100)58-25-15-27-88(58)71(102)56(31-43-36-78-50-23-12-9-20-46(43)50)85-67(98)54(30-42-35-77-49-22-11-8-19-45(42)49)82-64(95)51(24-13-14-26-73)80-66(97)53(29-41-34-76-48-21-10-7-18-44(41)48)83-68(99)55(32-59(75)90)81-63(94)47(74)38-89;3-2(4,5)1(6)7/h4-12,16-23,34-36,39,47,51-58,62,76-78,89H,3,13-15,24-33,37-38,73-74H2,1-2H3,(H2,75,90)(H,79,100)(H,80,97)(H,81,94)(H,82,95)(H,83,99)(H,84,101)(H,85,98)(H,86,96)(H,87,91)(H,92,93)(H,103,104);(H,6,7)/t39-,47-,51-,52-,53-,54-,55-,56-,57-,58-,62-;/m0./s1

Klucz InChI

VSUBSHMCMRUEAG-IQVZWRNHSA-N

Zastosowanie

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.

Działania biochem./fizjol.

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.
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Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 2

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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
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
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
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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