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F6312

Sigma-Aldrich

Fmoc-(S)-2-(4-pentenyl)Ala-OH

≥97%

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Synonym(s):
(S)-N-Fmoc-α-4-n-pentenylalanine, Fmoc-(S)-2-(4-pentenyl)alanine, Fmoc-(S)-2-amino-2-methyl-hept-6-enoic acid
Empirical Formula (Hill Notation):
C23H25NO4
CAS Number:
Molecular Weight:
379.45
NACRES:
NA.26

assay

≥97%

form

solid

reaction suitability

reaction type: Fmoc solid-phase peptide synthesis

mp

<30 °C

application(s)

peptide synthesis

functional group

Fmoc

storage temp.

−20°C

InChI

1S/C23H25NO4/c1-3-4-9-14-23(2,21(25)26)24-22(27)28-15-20-18-12-7-5-10-16(18)17-11-6-8-13-19(17)20/h3,5-8,10-13,20H,1,4,9,14-15H2,2H3,(H,24,27)(H,25,26)/t23-/m0/s1

InChI key

MRJFPZWLOJOINV-QHCPKHFHSA-N

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This Item
F6437F6687F6187
Sigma-Aldrich

F6312

Fmoc-(S)-2-(4-pentenyl)Ala-OH

Fmoc-(R)-2-(pentenyl)Ala-OH &#8805;97% (HPLC)

F6437

Fmoc-(R)-2-(pentenyl)Ala-OH

Fmoc-(S)-2-(7-octenyl)Ala-OH &#8805;97%

F6687

Fmoc-(S)-2-(7-octenyl)Ala-OH

Fmoc-(R)-2-(2-propenyl)Ala-OH &#8805;97%

F6187

Fmoc-(R)-2-(2-propenyl)Ala-OH

assay

≥97%

assay

≥97% (HPLC)

assay

≥97%

assay

≥97%

functional group

Fmoc

functional group

Fmoc

functional group

Fmoc

functional group

Fmoc

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

mp

<30 °C

mp

-

mp

-

mp

-

reaction suitability

reaction type: Fmoc solid-phase peptide synthesis

reaction suitability

reaction type: Fmoc solid-phase peptide synthesis

reaction suitability

reaction type: Fmoc solid-phase peptide synthesis

reaction suitability

reaction type: Fmoc solid-phase peptide synthesis

Application

Fmoc-(S)-2-(4-pentenyl)Ala-OH is a Fmoc-protected amino acid that can be used to create peptide libraries.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Z-selective olefin metathesis on peptides: Investigation of side chain influence, preorganization, and guidelines in substrate selection.
O?Leary D J and Grubbs R H
Amino Acids, 5, S13-S13 null
Young-Woo Kim et al.
Nature protocols, 6(6), 761-771 (2011-06-04)
This protocol provides a detailed procedure for the preparation of stapled α-helical peptides, which have proven their potential as useful molecular probes and as next-generation therapeutics. Two crucial features of this protocol are (i) the construction of peptide substrates containing

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