Chemical approaches to discover the full potential of peptide nucleic acids in biomedical applications

• Nikita Brodyagin,
• Martins Katkevics,
• Venubabu Kotikam,
• Christopher A. Ryan and
• Eriks Rozners

Beilstein J. Org. Chem. 2021, 17, 1641–1688, doi:10.3762/bjoc.17.116

• intercalation, triplex formation, and backbone chirality shifts [44]. A similar P-form helix having a wide and deep major groove and a shallow and narrow minor groove was also observed for an NMR solution structure of a self-complementary PNA–PNA duplex [45]. Taken together, these results confirmed that, while

Isolation and structure determination of a tetrameric sulfonyl dilithio methandiide in solution based on crystal structure analysis and ⁶Li/¹³C NMR spectroscopic data

• Jürgen Vollhardt,
• Hans Jörg Lindner and
• Hans-Joachim Gais

Beilstein J. Org. Chem. 2020, 16, 2057–2063, doi:10.3762/bjoc.16.172

• in THF solution in fast equilibrium with a further aggregate, which is stable only at low temperatures. Keywords: crystal structure; dilithio sulfonyl methandiide; NMR; solution structure; X-ray analysis; Introduction Functionalized dilithio methandiides I–III (Figure 1) are a fascinating class of

Design of a novel tryptophan-rich membrane-active antimicrobial peptide from the membrane-proximal region of the HIV glycoprotein, gp41

• Evan F. Haney,
• Leonard T. Nguyen,
• David J. Schibli and
• Hans J. Vogel

Beilstein J. Org. Chem. 2012, 8, 1172–1184, doi:10.3762/bjoc.8.130

• ; NMR solution structure; membrane interactions; peptides structure–function relationship; Introduction Antimicrobial peptides (AMPs) continue to attract significant attention as potential alternatives to conventional antibiotics. A large number of AMP sequences have been reported in the literature

• to the formation of insoluble peptide–lipid complexes. Unfortunately, due to the loss of CD signal in these samples, it is impossible to determine what type of secondary structure is present in these aggregates. NMR solution structure All the gp41w derivatives were examined by nuclear magnetic

• ), 25 mM SDS (green), 25 mM DPC (yellow) and 50% TFE (red). The panel on the right is the peptides in the presence of LUVs composed of ePC:ePG (violet), ePE:ePG (orange) or ePC:ePE (gray). All data are reported in units of mean residue ellipticity (MRE) with units of deg cm2 dmol−1 res−1. NMR solution