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Merck
CN

47431

Fmoc-Phe(4-I)-OH

≥97.0%

Synonym(s):

Fmoc-4-iodo-L-phenylalanine

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About This Item

Empirical Formula (Hill Notation):
C24H20INO4
CAS Number:
82565-68-2
Molecular Weight:
513.32
NACRES:
NA.26
PubChem Substance ID:
57650949
eCl@ss:
32160406
UNSPSC Code:
12352209
MDL number:
MFCD00672340
Beilstein/REAXYS Number:
4592723

Key Documents

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InChI

1S/C24H20INO4/c25-16-11-9-15(10-12-16)13-22(23(27)28)26-24(29)30-14-21-19-7-3-1-5-17(19)18-6-2-4-8-20(18)21/h1-12,21-22H,13-14H2,(H,26,29)(H,27,28)/t22-/m0/s1

SMILES string

OC(=O)[C@H](Cc1ccc(I)cc1)NC(=O)OCC2c3ccccc3-c4ccccc24

InChI key

LXOXXTQKKRJNNB-QFIPXVFZSA-N

assay

≥97.0%

reaction suitability

reaction type: Fmoc solid-phase peptide synthesis

application(s)

peptide synthesis

functional group

Fmoc

storage temp.

2-8°C

Quality Level

100

Related Categories

Other Notes

Synthesis of a phosphotyrosine mimetic; Building block employed for the synthesis of peptides carrying a radio-label

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
BCBW5767
BCBD8994V
BCBC8513
1345625
1317755

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R.E. Shute et al.
Tetrahedron Letters, 28, 3419-3419 (1987)
M.N. Qabar et al.
Tetrahedron, 53, 11171-11171 (1997)
Xiaoyan Mu et al.
Physical chemistry chemical physics : PCCP, 19(25), 16923-16933 (2017-06-21)
Four isomers of the radical cation of tripeptide phenylalanylglycyltryptophan, in which the initial location of the radical center is well defined, have been isolated and their collision-induced dissociation (CID) spectra examined. These ions, the π-centered [FGW
Sandra Ortega Ugalde et al.
Biochemical pharmacology, 177, 113938-113938 (2020-04-01)
Tuberculosis (TB) is a globally significant infective disease that is caused by a single infectious agent, Mycobacterium tuberculosis (Mtb). Because of the rise in the number of multidrug-resistant (MDR) TB strains, identification of alternative drug targets for the development of
Anirban Banerjee et al.
eLife, 2, e00594-e00594 (2013-05-25)
Pore-blocking toxins inhibit voltage-dependent K(+) channels (Kv channels) by plugging the ion-conduction pathway. We have solved the crystal structure of paddle chimera, a Kv channel in complex with charybdotoxin (CTX), a pore-blocking toxin. The toxin binds to the extracellular pore

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