288617-75-4 Usage
General Description
(S)-N-Fmoc-2-(7'-octenyl) alanine is a chemical compound that belongs to the class of amino acids. It is a derivative of alanine, an essential amino acid that plays a crucial role in the body's protein synthesis and overall health. The addition of the N-Fmoc and 7'-octenyl groups modify the structure and properties of alanine, making it useful in various applications in biochemistry and chemical biology. (S)-N-Fmoc-2-(7'-octenyl) alanine can be utilized in the synthesis of peptides and proteins, as well as in the study of protein-ligand interactions and enzyme kinetics. Its unique structure and reactivity make it a valuable tool for research in the fields of biochemistry and molecular biology.
Check Digit Verification of cas no
The CAS Registry Mumber 288617-75-4 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 2,8,8,6,1 and 7 respectively; the second part has 2 digits, 7 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 288617-75:
(8*2)+(7*8)+(6*8)+(5*6)+(4*1)+(3*7)+(2*7)+(1*5)=194
194 % 10 = 4
So 288617-75-4 is a valid CAS Registry Number.
InChI:InChI=1/C26H31NO4/c1-3-4-5-6-7-12-17-26(2,24(28)29)27-25(30)31-18-23-21-15-10-8-13-19(21)20-14-9-11-16-22(20)23/h3,8-11,13-16,23H,1,4-7,12,17-18H2,2H3,(H,27,30)(H,28,29)/t26-/m0/s1
288617-75-4Relevant articles and documents
Stabilized alpha helical peptides and uses thereof
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Sheet 2, (2016/05/19)
Novel polypeptides and methods of making and using the same are described herein. The polypeptides include cross-linking (“hydrocarbon stapling”) moieties to provide a tether between two amino acid moieties, which constrains the secondary structure of the polypeptide. The polypeptides described herein can be used to treat diseases characterized by excessive or inadequate cellular death.
Robust asymmetric synthesis of unnatural alkenyl amino acids for conformationally constrained α-helix peptides
Aillard, Boris,Robertson, Naomi S.,Baldwin, Adam R.,Robins, Siobhan,Jamieson, Andrew G.
supporting information, p. 8775 - 8782 (2014/12/11)
The efficient asymmetric synthesis of unnatural alkenyl amino acids required for peptide 'stapling' has been achieved using alkylation of a fluorine-modified NiII Schiff base complex as the key step.
