Nicole C. Thomas

TL;DR: A strategy for designing oligomers containing both α- and β-amino acid residues (“α/β-peptides”) that mimic several peptides derived from the three-helix bundle “Z-domain” scaffold that should enable the design of biostable α/ β- peptides that bind tightly and specifically to diverse targets of biomedical interest.

TL;DR: In this article , the authors evaluated the mechanism of action and anti-tumor efficacy of RTX1133, a potent, selective and non-covalent KRASG12D inhibitor.

TL;DR: Fragment growth supported by structural insights from X-ray crystallography coupled with optimization of pharmacokinetic properties aided the discovery of development candidate MRTX1719, a potent and selective binder to the PRMT5•MTA complex and selectively inhibitsPRMT5 activity in MTAP-deleted cells compared toMTAP-wild-type cells.

TL;DR: Structural trend supports the hypothesis that the Phe zipper motif has functional significance in two new quasiracemate crystals that contain the d form of the magainin 2 derivative along with an l-peptide in which one Ala has been replaced by a β-amino acid residue.

TL;DR: The study of α→β substitutions, involving both β3 and ACPC residues, is extended to short loops within a small tertiary motif and Crystal structures of three β‐containing Pin1 WW domain variants show that a native‐like tertiary structure is maintained in each case.