Yvonne AngellIpsen Pharmaceutical · Compound Discovery
Yvonne Angell
Ph.D.
About
15
Publications
765
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323
Citations
Introduction
Additional affiliations
September 1996 - May 1998
Position
- NIH Postdoctoral Research Fellow
Description
- I synthesized and characterized novel analogues of the protein Bovine Pancreatic Trypsin Inhibitor (BPTI), and investigated the effects of BPTI analogues on folding dynamics using biochemical and biophysical techniques.
January 1991 - September 1996
Position
- PhD Student
Description
- I synthesized amino acids the unusual amino acid MeBmt . I published the first complete solid-phase synthesis of an CsA analogue via on-resin cyclization and developed new conditions for coupling N-methylated amino acids on solid supports.
Publications
Publications (15)
Several approaches were investigated with the goal to obtain disulfide-free circularized analogues of the 58-residue small
protein bovine pancreatic trypsin inhibitor (BPTI). These approaches include (1) a semisynthesis that uses as a starting point
naturally occurring BPTI and takes advantage of the native proximity of the C- and N-termini; (2) a...
In an effort to identify new approaches to lead discovery a polyvalent assay was developed to allow identification of weak inhibitors. This approach involves the polyvalent display of a protein binder off a Tenta-gel scaffold and the generation of a polyvalent display of protein by biotinylation followed by complexation with fluorescently labeled s...
The solid-phase synthesis of a dipeptide derived 2-amino-3-oxohexahydroindolizino[8,7-b]indole-5-carboxylate system (IBTM) is described. The IBTM moiety is formed via a solid-phase mediated Pictet–Spengler reaction of N-terminal tryptophan and the 4-{N-[1-(4,4-dimethyl-2,6-dioxocyclohexylidene)-3-methylbutyl]amino}benzyl (Dmab) ester of Fmoc protec...
This study details a series of conditions that may be applied to ensure 'safe' incorporation of cysteine with minimal racemization during automated or manual solid-phase peptide synthesis. Earlier studies from our laboratories [Han et al. (1997) J. Org. Chem. 62, 4307-4312] showed that several common coupling methods, including those exploiting in...
The intrinsic fluorescence of tyrosine increases by a factor of approximately two when the carboxy group is liberated from a peptide bond by hydrolysis. The increase in fluorescence provides a novel way to monitor the hydrolysis of native tyrosine peptides that contain only proteinogenic amino acids. Thus, for example, the hydrolysis by HIV-1 prote...
Comparison of different coupling reagents for effective coupling of N-methylated, sterically hindered amino acids under solid-phase peptide synthesis (SPPS) conditions is described. Superior results were obtained with the coupling additive 1-hydroxy-7-azabenzotriazole (HOAt), as well as its uronium salt derivative (HATU), which both produced quanti...
Typescript. Thesis (Ph. D.)--University of Wisconsin--Madison, 1996. Includes bibliographical references (leaves 173-193).
