1335206-40-0

Usage

Uses

Used in Pharmaceutical Industry:
Glycine, N-[2-[[(9H-fluoren-9-ylMethoxy)carbonyl]aMino]ethyl]-N-(Methylsulfonyl)is used as a coupling reagent in peptide synthesis for the production of pharmaceutical compounds. Its unique structure allows for efficient and specific peptide synthesis, leading to the development of new and improved drugs.
Used in Biotechnology Industry:
In the biotechnology industry, Glycine, N-[2-[[(9H-fluoren-9-ylMethoxy)carbonyl]aMino]ethyl]-N-(Methylsulfonyl)is utilized as a coupling reagent in the synthesis of peptides for various biotechnological applications. Its stability and low toxicity make it suitable for use in the development of bioactive peptides and other biotechnological products.
Used in Peptide Synthesis:
Glycine, N-[2-[[(9H-fluoren-9-ylMethoxy)carbonyl]aMino]ethyl]-N-(Methylsulfonyl)is used as a coupling reagent in peptide synthesis to enhance the efficiency and specificity of the process. Its unique structure, including the Fmoc protecting group, aminoethyl group, and methylsulfonyl group, allows for the production of high-quality peptides with minimal side reactions and impurities.

Upstream product

• 169396-88-7 tert-butyl N-[2-(N-9-fluorenylmethoxycarbonyl)aminoethyl]glycinate hydrochloride 

Relevant academic research and scientific papers

Bioactivity improvement via display of the hydrophobic core of HYD1 in a cyclic β-hairpin-like scaffold, MTI-101

HYD1 is an all D-amino acid linear 10-mer peptide that was discovered by one-bead-one-compound screening. HYD1 has five hydrophobic amino acids flanked by polar amino acids. Alanine scanning studies showed that alternating hydrophobic amino acid residues and N- and C-terminal lysine side chains were contributors to the biological activity of the linear 10-mer analogs. This observation led us to hypothesize that display of the hydrophobic pentapeptide sequence of HYD1 in a cyclic beta-hairpin-like scaffold could lead to better bioavailability and biological activity. An amphipathic pentapeptide sequence was used to form an antiparallel strand and those strands were linked via dipeptide-like sequences selected to promote β-turns. Early cyclic analogs were more active but otherwise mimicked the biological activity of the linear HYD1 peptide. The cyclic peptidomimetics were synthesized using standard Fmoc solid phase synthesis to form linear peptides, followed by solution phase or on-resin cyclization. SAR studies were carried out with an aim to increase the potency of these drug candidates for the killing of multiple myeloma cells in vitro. The solution structures of 1, 5, and 10 were elucidated using NMR spectroscopy. 1H NMR and 2D TOCSY studies of these peptides revealed a downfield Hα proton chemical shift and 2D NOE spectral analysis consistent with a β-hairpin-like structure.

Integrin interaction inhibitors for the treatment of cancer

Integrin interaction inhibitors using a beta-turn promoter are described herein. These peptides are useful in treating cancer, such as multiple myeloma, by administering a therapeutically effective amount of the integrin interaction inhibitor. Data show that integrin interaction inhibitors act synergistically or additively interact with anti-proliferative agents such as doxorubicin, SAHA, arsenic trioxide, and etoposide.