The remarkable complexity of globular protein structures was first revealed about half a
century ago, when the crystal structure of myoglobin was determined at 2.4 Å. 1 In the …

This paper is the 28th consecutive installment of the annual review of research concerning
the endogenous opioid system, now spanning over a quarter-century of research. It …

The construction of bioactive peptides using β-amino acid-containing sequence patterns is a
very promising strategy to obtain analogues that exhibit properties of high interest for …

Despite various advantages, opioid peptides have been limited in their therapeutic uses due
to the main drawbacks in metabolic stability, blood-brain barrier permeability, and …

The application of endomorphins as clinical available analgesic drugs has been impeded by
their relatively poor receptor selectivity compared with alkaloid analgesics, rapid …

A new class of endomorphin-1 (EM-1) analogues were synthesized by introduction of novel
unnatural α-methylene-β-amino acids (Map) at position 3 or/and position 4. Their binding …

Recently we reported the synthesis and structure–activity study of endomorphin-1 (EM-1)
analogues containing novel, unnatural α-methylene-β-aminopropanoic acids (Map). In the …

The one-pot conversion of readily available α-amino acid into β-amino acid derivatives was
carried out in good yields. The method is a sequential process initiated by a tandem radical …

Herein we present the expedient synthesis of endomorphin-1 analogues containing
stereoisomeric β2-homo-Freidinger lactam-like scaffolds ([Amo2] EM), and we discuss …

β-Amino acids are being increasingly used in the design of bioactive ligands and more
recently in the generation of novel biomaterials. Peptides containing either individual β …