1251904-51-4

Basic information

• Product Name: (S)-N-FMoc-2-(5'-pentenyl)glycine
• Synonyms: (S)-N-FMoc-2-(5'-pentenyl)glycine;(S)-N-Fmoc-2-(5'-hexyl)glycine;(S)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)oct-7-enoic acid;(S)-N-FMOC-2-(5'-HEXENYL)GLYCINE;7-Octenoic acid, 2-[[(9H-fluoren-9-ylmethoxy)carbonyl]amino]-, (2S)-
• CAS NO: 1251904-51-4
• Molecular Formula: C₂₃H₂₅NO₄
• Molecular Weight: 365.42232
• Mol File: 1251904-51-4.mol
• Article Data: 1

Chemical Properties

• Boiling Point: 603.1±55.0 °C(Predicted)
• Appearance: /
• Density: 1.184±0.06 g/cm3(Predicted)
• Storage Temp.: 2-8°C
• PKA: 3.90±0.21(Predicted)
• CAS DataBase Reference: (S)-N-FMoc-2-(5'-pentenyl)glycine(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-N-FMoc-2-(5'-pentenyl)glycine(1251904-51-4)
• EPA Substance Registry System: (S)-N-FMoc-2-(5'-pentenyl)glycine(1251904-51-4)

Safety Data

• Hazardous Substances Data: 1251904-51-4(Hazardous Substances Data)

Usage

General Description

(S)-N-Fmoc-2-(5'-pentenyl)glycine is a chemical compound used in the field of organic chemistry. It is commonly utilized in the synthesis of peptides and other bioactive molecules. The compound consists of a glycine molecule with a pentenyl group attached at the 5' position, as well as an Fmoc (9-fluorenylmethoxycarbonyl) protecting group. (S)-N-Fmoc-2-(5'-pentenyl)glycine can be used as a building block in the creation of various peptide chains, allowing for the formation of diverse and complex molecules with specific biological functions. Its unique structure and reactivity make it a valuable tool in the development of new pharmaceuticals and biologically active compounds.

Upstream product

• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 848777-71-9 (S)-2-(N-benzyloxycarbonyl)amino-7-octenoic acid 

Relevant articles and documents

Potent macrocyclic inhibitors of insulin-regulated aminopeptidase (IRAP) by olefin ring-closing metathesis

Macrocyclic analogues of angiotensin IV (Ang IV, Val1-Tyr 2-Ile3-His4-Pro5-Phe6) targeting the insulin-regulated aminopeptidase (IRAP) have been designed, synthesized, and evaluated biologically. Replacement of His4-Pro 5-Phe6 by a 2-(aminomethyl)phenylacetic acid (AMPAA) moiety and of Val1 and Ile3 by amino acids bearing olefinic side chains followed by macrocyclization provided potent IRAP inhibitors. The impact of the ring size and the type (saturated versus unsaturated), configuration, and position of the carbon-carbon bridge was assessed. The ring size generally affects the potency more than the carbon-carbon bond characteristics. Replacing Tyr2 by β3hTyr or Phe is accepted, while N-methylation of Tyr 2 is deleterious for activity. Removal of the carboxyl group in the C-terminal slightly reduced the potency. Inhibitors 7 (Ki = 4.1 nM) and 19 (Ki = 1.8 nM), both encompassing 14-membered ring systems connected to AMPAA, are 10-fold more potent than Ang IV and are also more selective over aminopeptidase N (AP-N). Both compounds displayed high stability against proteolysis by metallopeptidases.