Synthesis and conformational characterization in the solid state of peptides consisting of L-phenylalanyl-L-phenylalanylglycyl and L-phenylalanyl-L-leucylglycyl residues
✍ Scribed by Ryoichi Katakai; Yoko Nakayama
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1981
- Tongue
- English
- Weight
- 435 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
Two series of peptides containing L‐phenylalanine, Nps‐(L‐Phe‐L‐Phe‐Gly)~n~‐OEt (n = 1–6) and Nps‐(L‐Phe‐L‐Leu‐Gly)~n~‐OEt (n = 1–7), were prepared by the fragment‐condensation method using the tripeptide N‐hydroxysuccinimide esters. Conformational characterization of these peptides in the solid state was performed by ir spectroscopy and x‐ray powder diffraction measurement. The peptides Nps‐(L‐Phe‐L‐Phe‐Gly)~n~‐OEt take the β‐structure, but the pentadecapeptide and higher peptides of Nps‐(L‐Phe‐L‐Leu‐Gly)~n~‐OEt form the α‐helix, although the lower homologs take the β‐structure.
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## Abstract Experimental vibrational spectroscopic studies and density functional theory (DFT) calculations of the di‐amino acid peptide derivatives α‐ and β‐__N__‐acetyl‐L‐Asp‐L‐Glu have been undertaken. Raman and infrared spectra have been recorded for samples in the solid state. DFT simulations
## Abstract The ^13^C chemical shifts and spin‐lattice relaxation times are reported for __cyclo__(L‐Pro‐L‐Leu) and __cyclo__(L‐Pro‐D‐Leu). The chemical shifts of the D and L leucyl residues in the cyclic peptides differ from each other by 1.8 and 3.6 parts per million for the α and β carbons, resp