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Merck

26569

2-Chlorotrityl chloride

≥97.0% (AT)

Synonym(s):

Chloro(2-chlorophenyl)diphenylmethane

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About This Item

Empirical Formula (Hill Notation):
C19H14Cl2
CAS Number:
Molecular Weight:
313.22
UNSPSC Code:
12352100
NACRES:
NA.22
PubChem Substance ID:
EC Number:
255-647-3
Beilstein/REAXYS Number:
1983914
MDL number:
Assay:
≥97.0% (AT)
Form:
solid
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Quality Level

assay

≥97.0% (AT)

form

solid

mp

130-135 °C

functional group

chloro, phenyl

SMILES string

Clc1ccccc1C(Cl)(c2ccccc2)c3ccccc3

InChI

1S/C19H14Cl2/c20-18-14-8-7-13-17(18)19(21,15-9-3-1-4-10-15)16-11-5-2-6-12-16/h1-14H

InChI key

JFLSOKIMYBSASW-UHFFFAOYSA-N

Application

2-Chlorotrityl chloride was used to obtain protected peptide fragments that can be applied to the preparation of head-to-tail cyclopeptides or to condensation of peptidic fragments.

Other Notes

Protecting group reagent for carboxylic acids forming esters which are cleaved mildly.


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pictograms

CorrosionExclamation mark

signalword

Warning

Hazard Classifications

Eye Irrit. 2 - Met. Corr. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Storage Class

11 - Combustible Solids



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Jie Luo et al.
Journal of the American Society for Mass Spectrometry, 30(9), 1643-1653 (2019-06-07)
Chemical cross-linking combined with mass spectrometry (CL-MS) is a powerful method for characterizing the architecture of protein assemblies and for mapping protein-protein interactions. Despite its proven utility, confident identification of cross-linked peptides remains a formidable challenge, especially when the peptides
K Barlos et al.
International journal of peptide and protein research, 37(6), 513-520 (1991-06-01)
The esterification of 2-chlorotrityl chloride resin with Fmoc-amino acids in the presence of DIEA is studied under various conditions. High esterification yields are obtained using 0.6 equiv. Fmoc-amino acid/mmol resin in DCM or DCE, in 25 min, at room temperature.
Shinichiro F Ichise et al.
Acta biomaterialia, 94, 361-371 (2019-06-15)
Collagen is the most abundant protein in the animal kingdom and has a unique triple-helical structure. It not only provides mechanical strength to tissues, but also performs specific biological functions as a multifaceted signaling molecule. Animal-derived collagen is therefore widely