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B8435

Sigma-Aldrich

BiCAPPA

≥97% (HPLC), solid

Synonym(s):

N,N′-Bis(6-chloro-2-methoxy-9-acridinyl)-1,4-piperazinedipropanamine

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About This Item

Empirical Formula (Hill Notation):
C38H40Cl2N6O2
CAS Number:
119662-55-4
Molecular Weight:
683.67
MDL number:
MFCD07370130
UNSPSC Code:
12352202
PubChem Substance ID:
24724426
NACRES:
NA.77

Assay

≥97% (HPLC)

form

solid

storage condition

under inert gas

color

yellow

solubility

DMSO: ~10 mg/mL

storage temp.

2-8°C

SMILES string

COc1ccc2nc3cc(Cl)ccc3c(NCCCN4CCN(CCCNc5c6ccc(Cl)cc6nc7ccc(OC)cc57)CC4)c2c1

InChI

1S/C38H40Cl2N6O2/c1-47-27-7-11-33-31(23-27)37(29-9-5-25(39)21-35(29)43-33)41-13-3-15-45-17-19-46(20-18-45)16-4-14-42-38-30-10-6-26(40)22-36(30)44-34-12-8-28(48-2)24-32(34)38/h5-12,21-24H,3-4,13-20H2,1-2H3,(H,41,43)(H,42,44)

InChI key

GUTKNTSGEOMFPZ-UHFFFAOYSA-N

Biochem/physiol Actions

Inhibitor of the formation of abnormal ß-rich isoform of prion protein PrPSc.

Pictograms

Exclamation mark
GHS07

Signal Word

Warning

Hazard Statements

H315,H319,H335

Precautionary Statements

P261 - P305 + P351 + P338

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Certificates of Analysis (COA)

Lot/Batch Number
114K4617

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Barnaby C H May et al.
Proceedings of the National Academy of Sciences of the United States of America, 100(6), 3416-3421 (2003-03-11)
Prion diseases are characterized by an accumulation of PrP(Sc), a misfolded isoform of the normal cellular prion protein, PrP(C). We previously reported the bioactivity of acridine-based compounds against PrP(Sc) replication in scrapie-infected neuroblastoma cells and now report the improved potency
Christopher A Ross et al.
Nature medicine, 10 Suppl, S10-S17 (2004-07-24)
Neurodegenerative diseases such as Alzheimer's disease (AD), Parkinson's disease (PD), Huntington's disease (HD), amyotrophic lateral sclerosis (ALS) and prion diseases are increasingly being realized to have common cellular and molecular mechanisms including protein aggregation and inclusion body formation. The aggregates

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