62530-41-0

Basic information

• Product Name: Boc-Tyr(O-t-Bu)-Glu-Gly-OH
• Synonyms: Boc-Tyr(O-t-Bu)-Glu-Gly-OH
• CAS NO: 62530-41-0
• Molecular Weight: 451.52
• Mol File: 62530-41-0.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: Boc-Tyr(O-t-Bu)-Glu-Gly-OH(CAS DataBase Reference)
• NIST Chemistry Reference: Boc-Tyr(O-t-Bu)-Glu-Gly-OH(62530-41-0)
• EPA Substance Registry System: Boc-Tyr(O-t-Bu)-Glu-Gly-OH(62530-41-0)

Safety Data

• Hazardous Substances Data: 62530-41-0(Hazardous Substances Data)

Upstream product

• 85541-33-9 N-t-butoxycarbonyl-O-t-butyl-L-tyrosylglycine methyl ester 
• 47375-34-8 Boc-Tyr(t-Bu)-OH 

Downstream Products

• 264921-62-2 N-[1S-(1α,2α,3β)]-2-[N-(tert-butoxycarbonyl)-L-tyrosine-t-butyl ether-L-glycine-L-glycine]-3-phenylcyclopropane-1-N-(tert-butoxycarbonyl)-L-leucine methyl ester 

Relevant articles and documents

Preparation and evaluation at the delta opioid receptor of a series of linear Leu-enkephalin analogues obtained by systematic replacement of the amides

Leu-enkephalin analogues, in which the amide bonds were sequentially and systematically replaced either by ester or N-methyl amide bonds, were prepared using classical organic chemistry as well as solid phase peptide synthesis (SPPS). The peptidomimetics were characterized using competition binding, ERK1/2 phosphorylation, receptor internalization, and contractility assays to evaluate their pharmacological profile over the delta opioid receptor (DOPr). The lipophilicity (LogD7.4) and plasma stability of the active analogues were also measured. Our results revealed that the last amide bond can be successfully replaced by either an ester or an N-methyl amide bond without significantly decreasing the biological activity of the corresponding analogues when compared to Leu-enkephalin. The peptidomimetics with an N-methyl amide function between residues Phe and Leu were found to be more lipophilic and more stable than Leu-enkephalin. Findings from the present study further revealed that the hydrogen-bond donor properties of the fourth amide of Leu-enkephalin are not important for its biological activity on DOPr. Our results show that the systematic replacement of amide bonds by isosteric functions represents an efficient way to design and synthesize novel peptide analogues with enhanced stability. Our findings further suggest that such a strategy can also be useful to study the biological roles of amide bonds.