Her research has contributed to three different areas of chemical biology: protein-DNA recognition and transcriptional activation; the development of miniature proteins that bind specifically and with high affinity to protein and DNA; and the development of β-peptides as protein ligands and as building blocks of protein-like architectures.
He has achieved his most important results by use of spectroscopy: he has studied bioactive peptides with CD, NMR spectroscopy and molecular modelling.
In molecular biology, the bombinin family of antimicrobial peptides includes the bombinin and maximin proteins from Bombina maxima (Giant fire-bellied toad).
The key amino acids of the BSCI peptides required for activity have been identified, and the tripeptide AcNH-Trp-Val-Gln-OH was shown to itself be a BSCI in the low micromolar range.
The method was first used by Max Bergmann and Leonidas Zerwas in 1932 for the synthesis of peptides.
Cupiennins are a group of small cytolytic peptides from the venom of the wandering spider Cupiennius salei.
Efrapeptins are peptides made by Tolypocladium that have antifungal, insecticidal, and mitochondrial ATPase inhibitory activities.
That observation, called MHC restriction, led to a conundrum; namely, that the ability of a T cell to recognize foreign antigen also required that it recognize "self." With Paul M. Allen, Ph.D., the Robert L. Kroc Professor at Washington University School of Medicine, Unanue discovered that peptides from foreign antigens were bound to a group of molecules known as the major histocompatibility complex (MHC).
IDE, which migrates at 110 kDa during gel electrophoresis under denaturing conditions, has since been shown to have additional substrates, including the signaling peptides glucagon, TGF alpha, and β-endorphin.
Lourdes J. Cruz is a biochemist whose research has contributed to the understanding of the biochemistry of toxic peptides from the venom of fish-hunting Conus marine snails.
Their discovery represented the first example of an antimicrobial peptide produced in the skin of an animal, and complemented prior studies by Hans Boman of Sweden in the Cecropia moth, and Robert Lehrer (US) in rabbit white blood cells (defensins), supporting the widespread existence of antimicrobial peptides throughout nature.
He is known for his work on innate immunity and antimicrobial peptides including the discovery of Magainin from the frog Xenopus laevis.
MOWSE, a method for identification of proteins from the molecular weight of peptides created by proteolytic digestion
ENOD40 — is an early nodulin gene, hence ENOD, that putatively encodes two small peptides, one of 12 and the other of 18 amino acid residues.
Enzymes responsible for processing of POMC peptides include prohormone convertase 1 (PC1), prohormone convertase 2 (PC2), carboxypeptidase E (CPE), peptidyl α-amidating monooxygenase (PAM), N-acetyltransferase (N-AT), and prolylcarboxypeptidase (PRCP).
The relaxin-like peptide family belongs in the insulin superfamily and consists of 7 peptides of high structural but low sequence similarity; relaxin-1 (RLN1), 2 (RLN2) and 3 (RLN3), and the insulin-like (INSL) peptides, INSL3, INSL4, INSL5 and INSL6.
Because traditional methods of chemical discovery and selection relied on "natural" pathways (those formed by sources found in the wild and brought into the library), creation of the requisite number of peptides for new drug discovery was impractical.
Thiolactone rings can also be found in peptides synthesized by bacteria such as Staphylococcus aureus in order to regulate their quorum-sensing system.