138774-93-3 Usage
Description
Fmoc-D-1-Naphthylalanine, also known as N-(9-fluorenylmethoxycarbonyl)-D-1-naphthylalanine, is an amino acid derivative characterized by its white powder form. It is a synthetic compound that plays a significant role in the field of chemical synthesis and peptide chemistry due to its unique structural properties.
Uses
Used in Chemical Synthesis:
Fmoc-D-1-Naphthylalanine is used as a building block for the synthesis of various complex organic molecules. Its unique naphthyl group provides specific structural and functional characteristics that can be exploited in the design and synthesis of novel compounds with potential applications in various industries.
Used in Peptide Chemistry:
In the field of peptide chemistry, Fmoc-D-1-Naphthylalanine is utilized as a non-natural amino acid for the construction of peptide sequences. Its incorporation into peptide chains can lead to the development of new bioactive peptides with specific biological activities, such as those with enhanced stability, binding affinity, or pharmacokinetic properties.
Used in Pharmaceutical Industry:
Fmoc-D-1-Naphthylalanine is used as a key component in the development of new drugs and therapeutic agents. Its unique structural features can be employed to design and synthesize novel drug candidates with improved efficacy, selectivity, and pharmacological properties.
Used in Research and Development:
In the research and development sector, Fmoc-D-1-Naphthylalanine serves as an essential tool for studying the structure-activity relationships of various biologically active molecules. Its incorporation into peptide sequences can help researchers understand the role of specific amino acid residues in the biological activity of peptides and proteins.
Used in Material Science:
Fmoc-D-1-Naphthylalanine can also be used in the development of novel materials with specific properties, such as those with enhanced optical, electronic, or mechanical characteristics. Its unique naphthyl group can be exploited to design and synthesize new materials with potential applications in various industries, including electronics, energy, and environmental protection.
Check Digit Verification of cas no
The CAS Registry Mumber 138774-93-3 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,3,8,7,7 and 4 respectively; the second part has 2 digits, 9 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 138774-93:
(8*1)+(7*3)+(6*8)+(5*7)+(4*7)+(3*4)+(2*9)+(1*3)=173
173 % 10 = 3
So 138774-93-3 is a valid CAS Registry Number.
InChI:InChI=1/C28H23NO4/c30-27(31)26(16-19-10-7-9-18-8-1-2-11-20(18)19)29-28(32)33-17-25-23-14-5-3-12-21(23)22-13-4-6-15-24(22)25/h1-15,25-26H,16-17H2,(H,29,32)(H,30,31)/t26-/m1/s1
138774-93-3Relevant articles and documents
Novel selective inhibitors of the interaction of individual nuclear hormone receptors with a mutually shared steroid receptor coactivator 2
Geistlinger, Timothy R.,Guy, R. Kiplin
, p. 6852 - 6853 (2007/10/03)
Nuclear hormone receptor (NR) signaling, currently a therapeutic target in multiple diseases, involves an ordered series of protein interactions to regulate transcription in response to changing hormone levels. Later steps in the process of ligand-dependent signaling are driven by a highly conserved interaction between the NRs and the steroid receptor coactivators (SRCs) that is effected by a conserved interaction motif (L1XXL2L3), known as an NR box. Using computational design and combinatorial chemistry, we have produced novel ∞-helical proteomimetics of the second NR box of SRC2 that exploit structural differences between human estrogen receptor ∞ (hER∞), human estrogen receptor β (hERβ), and human thyroid hormone receptor β (hTRβ). The resulting library sequentially replaced each leucine with non-natural side chains. Screening this library using a quantitative competition assay revealed compounds that selectively inhibit the interaction of SRC2-2 with each individual NR in preference to its interaction with the other NR. This approach generated highly selective compounds from one that had no specificity for a particular family member. These compounds represent the first family-member-selective competitive inhibitors of the protein interactions of transcription factors. Copyright
Cyclic peptides as selective tachykinin antagonists
Williams,Curtis,McKnight,Maguire,Young,Veber,Baker
, p. 2 - 10 (2007/10/02)
Twenty homodetic cyclic peptides based on the C-terminal sequence of substance P were prepared (Table I) by a combination of solid-phase techniques and cyclizations using azide coupling procedures. Incorporation of dipeptide mimics based on substituted γ-
