288617-71-0 Usage
Description
(S)-N-Fmoc-2-(2'-propylenyl)alanine is a specialized amino acid derivative used in the field of peptide chemistry. It is characterized by the presence of an olefinic side chain, which allows for the creation of stable peptide structures through a process known as peptide stapling. This unique property makes it a valuable compound for the development of novel therapeutic peptides with enhanced stability and cellular uptake.
Uses
Used in Pharmaceutical Industry:
(S)-N-Fmoc-2-(2'-propylenyl)alanine is used as a building block for the synthesis of stapled peptides. The incorporation of this amino acid into a peptide sequence, along with another of the same or a derivative with a different length of the olefinic side chain, enables the formation of a stable alpha-helical structure through a ring-closing metathesis reaction using Grubbs' catalyst. This process results in a stapled peptide macrocycle, which has been shown to exhibit increased proteolytic stability and enhanced cellular uptake, making it a promising approach for the development of new drugs with improved efficacy and safety profiles.
Used in Research and Development:
In the field of research and development, (S)-N-Fmoc-2-(2'-propylenyl)alanine serves as an essential tool for studying the structure-function relationships of peptides and proteins. By incorporating this amino acid into peptide sequences, researchers can investigate the effects of peptide stapling on protein-protein interactions, protein stability, and cellular signaling pathways. This information can be crucial for understanding the underlying mechanisms of various diseases and for the design of targeted therapeutic strategies.
Used in Drug Design and Optimization:
(S)-N-Fmoc-2-(2'-propylenyl)alanine is used as a key component in the design and optimization of peptide-based drugs. The ability to create stable alpha-helical structures through peptide stapling allows for the development of peptides with enhanced biological activity and selectivity. This can lead to the discovery of novel therapeutic agents with improved pharmacokinetic properties, reduced off-target effects, and increased resistance to degradation by proteolytic enzymes.
Check Digit Verification of cas no
The CAS Registry Mumber 288617-71-0 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 1 respectively.
Calculate Digit Verification of CAS Registry Number 288617-71:
(8*2)+(7*8)+(6*8)+(5*6)+(4*1)+(3*7)+(2*7)+(1*1)=190
190 % 10 = 0
So 288617-71-0 is a valid CAS Registry Number.
InChI:InChI=1/C21H21NO4/c1-3-12-21(2,19(23)24)22-20(25)26-13-18-16-10-6-4-8-14(16)15-9-5-7-11-17(15)18/h3-11,18H,1,12-13H2,2H3,(H,22,25)(H,23,24)/t21-/m0/s1
288617-71-0Relevant articles and documents
PEPTIDOMIMETIC INHIBITORS OF THE WDR5-MLL INTERACTION
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Paragraph 0240; 0244; 0245, (2018/12/13)
The present disclosure provides compounds represented by Formula I: and the pharmaceutically acceptable salts and solvates thereof, wherein R1, R2, R3a, R3b, R4a, R4b, R5a, and R5b are as defined as set forth in the specification. The present disclosure also provides compounds of Formula I for use to treat a condition, disease, or disorder responsive to inhibition of the WDR5 interaction with its binding partners including, but not limited to, the WDR5-MLL protein-protein interaction.
Influence of α-methylation in constructing stapled peptides with olefin metathesis
Zhang, Qingzhou,Shi, Xiaodong,Jiang, Yanhong,Li, Zigang
, p. 7621 - 7626 (2014/12/11)
Ring-closing metathesis is commonly utilized in peptide macro-cyclization. The influence of α-methylation of the amino acids bearing the olefin moieties has never been systematically studied. In this report, controlled reactions unambiguously indicate that α-methylation at the N-terminus of the metathesis sites is crucial for this reaction to occur. Also, we first elucidated that the E-isomers of stapled peptides are significantly more helical than the Z-isomers.
An all-hydrocarbon cross-linking system for enhancing the helicity and metabolic stability of peptides [8]
Schafmeister, Christian E.,Po, Julia,Verdine, Gregory L.
, p. 5891 - 5892 (2007/10/03)
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