Fmoc-Ala(alpha-cyclopropyl)-OH
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Fmoc-Ala(alpha-cyclopropyl)-OH

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Category
Fmoc-Amino Acids
Catalog number
BAT-008409
CAS number
1926163-87-2
Molecular Formula
C21H21NO4
Molecular Weight
351.4
IUPAC Name
(2S)-2-cyclopropyl-2-(9H-fluoren-9-ylmethoxycarbonylamino)propanoic acid
Synonyms
DS-019127
Density
1.3±0.1 g/cm3
Boiling Point
575.7±33.0 °C at 760 mmHg
InChI
InChI=1S/C21H21NO4/c1-21(19(23)24,13-10-11-13)22-20(25)26-12-18-16-8-4-2-6-14(16)15-7-3-5-9-17(15)18/h2-9,13,18H,10-12H2,1H3,(H,22,25)(H,23,24)/t21-/m0/s1
InChI Key
SBWCIRABWAINIK-NRFANRHFSA-N
Canonical SMILES
CC(C1CC1)(C(=O)O)NC(=O)OCC2C3=CC=CC=C3C4=CC=CC=C24

Fmoc-Ala(alpha-cyclopropyl)-OH, a specialized amino acid derivative utilized in peptide synthesis and biochemical research, serves as a versatile component with diverse applications. Explore its key uses through intriguing descriptions crafted with high perplexity and burstiness:

Peptide Synthesis: Within solid-phase peptide synthesis, Fmoc-Ala(alpha-cyclopropyl)-OH emerges as a pivotal addition, infusing non-standard amino acids into peptide chains. The unique cyclopropyl group lends structural rigidity, potentially molding peptide conformations. This nuanced approach is fundamental in sculpting peptides with tailored conformational traits, essential for unraveling biochemical intricacies.

Drug Development: Delving into pharmaceutical realms, integrating Fmoc-Ala(alpha-cyclopropyl)-OH into peptides sparks innovation in crafting novel peptide-based therapeutics. The altered peptide may exhibit shifted pharmacokinetics and heightened resilience against enzymatic breakdown, bolstering the durability of drug candidates. This strategic inclusion holds promise for enhancing drug efficacy and resilience.

Protein Engineering: Navigating the terrain of protein engineering, the incorporation of Fmoc-Ala(alpha-cyclopropyl)-OH unveils a realm of possibilities in probing structural modifications' impact on protein functionality. Infusing this amino acid into protein sequences enables researchers to gauge alterations in activity, binding affinity, and stability. This exploration aids in deciphering protein dynamics and molding proteins with desired attributes, steering towards tailored functionalities.

Biophysical Studies: Embracing biophysical inquiries, this amino acid derivative proves invaluable in unraveling peptide-protein interactions and folding mechanisms. The addition of the cyclopropyl group introduces precise steric constraints, shedding light on folding pathways and interaction surfaces of peptides. This data serves as a cornerstone in elucidating the principles governing protein structure and function, unveiling insights through a lens of intricate molecular dynamics.

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