کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1406149 | 1501778 | 2013 | 11 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Conformational studies of γ-turn in pseudopeptides containing α-amino acid and conformationally constrained meta amino benzoic acid/meta nitro aniline Conformational studies of γ-turn in pseudopeptides containing α-amino acid and conformationally constrained meta amino benzoic acid/meta nitro aniline](/preview/png/1406149.png)
Reverse turns (commonly β-turns and γ-turns), a common motif in proteins and peptides, have attracted attention due to their relevance in a wide variety of biological processes. In an attempt to artificially imitate and stabilize these turns in short acyclic peptides, a series of N-terminally protected pseudopeptides comprising of an α-amino acid and conformationally constrained meta amino benzoic acid (mABA)/meta nitro aniline (mNA) (peptides I–VI) have been synthesized. The molecules were well characterized by various spectroscopic techniques and subjected to a systematic conformational analysis. Our experimental results reveal that only pseudopeptides I and II with methyl as the sidechain, tertiary butyloxy carbonyl as the N-terminal protecting group and (mABA)/(mNA) at the C-terminus adopt γ-turn conformations in solid state as well as in solution. Even slight modification of any of the stated conditions donot support the formation of this γ-turn architecture in the solid state. Interestingly, the peptides III–V which displays extended conformation in solid state forms γ-turn structure in solution. Thus this result reflects the importance of co-operative steric interactions amongst various amino acid residues in stabilizing a particular conformation in peptides in different phases (solid and solution). This report may open a new avenue in introducing γ-turn motifs within the bioactive conformation of selected peptides.
► Pseudopeptides I & II with appropriate N & C terminal protecting groups adopt γ-turn conformation.
► Pseudopeptides III–V displaying extended conformation in solid state forms γ-turn in solution.
► Importance of steric interactions amongst amino acid residues is crucial for γ-turn stabilization.
► The work may open a new avenue in introducing γ-turn within the bioactive conformation of peptides.
Journal: Journal of Molecular Structure - Volume 1036, 27 March 2013, Pages 350–360