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C 11 /C 9 Helical Folding in αβ Hybrid Peptides Containing 1‐Amino‐cyclohexane acetic acid (β 3, 3 ‐Ac 6 c)
Author(s) -
Wani Naiem Ahmad,
Raghothama Srinivasarao,
Singh Umesh Prasad,
Rai Rajkishor
Publication year - 2017
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201700265
Subject(s) - intramolecular force , tetrapeptide , chemistry , pentapeptide repeat , dipeptide , hydrogen bond , folding (dsp implementation) , stereochemistry , crystallography , molecule , peptide , amino acid , cyclohexane , biochemistry , organic chemistry , electrical engineering , engineering
Abstract The present study describes the solid‐state conformation of αβ hybrid peptides, Boc‐Leu‐β 3, 3 ‐Ac 6 c‐OH, P1 ; Boc‐Leu‐β 3, 3 ‐Ac 6 c‐Leu‐β 3, 3 ‐Ac 6 c‐OMe, P2 ; and Boc‐Leu‐β 3, 3 ‐Ac 6 c‐Leu‐β 3, 3 ‐Ac 6 c‐Leu‐OMe, P3 . The dipeptide P1 adopts extended conformations, whereas tetrapeptide P2 and pentapeptide P3 favor a helical conformation stabilized by mixed types of C 11 /C 9 intramolecular hydrogen bonds. In peptide P3 , the amino group of β 3, 3 ‐Ac 6 c(2) and β 3, 3 ‐Ac 6 c(4) residues occupies axial orientation, whereas in P2 it occupies axial and equatorial orientations for residues β 3, 3 ‐Ac 6 c(2) and β 3, 3 ‐Ac 6 c(4), respectively. The self‐assembly of P3 forms channels filled with solvent molecules that present interesting patterns.