Chemistry - A European Journal
Chemistry - A European Journal
5 years ago

C11/C9 Helical Folding in αβ Hybrid Peptides Containing 1-Amino-cyclohexane acetic acid (β3, 3-Ac6c)

C11/C9 Helical Folding in αβ Hybrid Peptides Containing 1-Amino-cyclohexane acetic acid (β3, 3-Ac6c)
Naiem Ahmad Wani, Rajkishor Rai, Umesh Prasad Singh, Srinivasarao Raghothama
The present study describes the solid-state conformation of αβ hybrid peptides, Boc-Leu-β3, 3-Ac6c-OH, P1; Boc-Leu-β3, 3-Ac6c-Leu-β3, 3-Ac6c-OMe, P2; and Boc-Leu-β3, 3-Ac6c-Leu-β3, 3-Ac6c-Leu-OMe, P3. The dipeptide P1 adopts extended conformations, whereas tetrapeptide P2 and pentapeptide P3 favor a helical conformation stabilized by mixed types of C11/C9 intramolecular hydrogen bonds. In peptide P3, the amino group of β3, 3-Ac6c(2) and β3, 3-Ac6c(4) residues occupies axial orientation, whereas in P2 it occupies axial and equatorial orientations for residues β3, 3-Ac6c(2) and β3, 3-Ac6c(4), respectively. The self-assembly of P3 forms channels filled with solvent molecules that present interesting patterns. Stable helices: Mixed C11/C9 intramolecular hydrogen bonds with opposite directionalities stabilize the helical conformation in αβ hybrid peptides.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/chem.201700265

You might also like
Discover & Discuss Important Research

Keeping up-to-date with research can feel impossible, with papers being published faster than you'll ever be able to read them. That's where Researcher comes in: we're simplifying discovery and making important discussions happen. With over 19,000 sources, including peer-reviewed journals, preprints, blogs, universities, podcasts and Live events across 10 research areas, you'll never miss what's important to you. It's like social media, but better. Oh, and we should mention - it's free.

  • Download from Google Play
  • Download from App Store
  • Download from AppInChina

Researcher displays publicly available abstracts and doesn’t host any full article content. If the content is open access, we will direct clicks from the abstracts to the publisher website and display the PDF copy on our platform. Clicks to view the full text will be directed to the publisher website, where only users with subscriptions or access through their institution are able to view the full article.