Please use this identifier to cite or link to this item: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/3234
Title: Helices with additional H‐bonds: crystallographic conformations of α,γ‐hybrid peptides helices composed of β‐hydroxy γ‐amino acids (statines)
Authors: Malik, Ankita
Kumar, Mothukuri Ganesh
BANDYOPADHYAY, ANUPAM
GOPI, HOSAHUDYA N.
Dept. of Chemistry
Keywords: H-bonds
β‐hydroxy
γ‐amino
Amino acids
Conformations H-bonds
Peptides X-ray
2017
Issue Date: Jan-2017
Publisher: Wiley
Citation: Biopolymers, 108(1), e22978.
Abstract: β‐Hydroxy‐γ‐amino acids (Statines) are a class of naturally occurring non‐ribosomal amino acids frequently found in many peptide natural products. Peptidomimetics constituted with statines have been used as inhibitors for various aspartic acid proteases. In contrast to the synthetic γ‐amino acids, very little is known about the folding behavior of these naturally occurring β‐hydroxy γ‐amino acids. To understand the folding behavior of statines, three α,γ‐hybrid peptides P1 (Ac‐Aib‐γPhe‐Aib‐(R, S)Phesta‐Aib‐γPhe‐Aib‐CONH2), P2 (Ac‐Aib‐γPhe‐Aib‐(S, S)Phesta‐Aib‐γPhe‐Aib‐CONH2), and P3 (Ac‐Aib‐γPhe‐Aib‐(S, S)Phesta‐Aib‐(S, S)Phesta‐Aib‐CONH2) were synthesized on solid phase and their helical conformations in single crystals were studied. Results suggest that both syn and anti diastereoisomers of statines can be accommodated into the helix without deviating overall helical conformation of α,γ‐hybrid peptides. In comparison with syn diastereoisomer, the anti diastereoisomer was found to be directly involved in the intramolecular H‐bonding with the backbone carbonyl groups (i to i + 3) similar to the backbone amide NHs in the helix.
URI: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/3234
https://doi.org/10.1002/bip.22978
ISSN: 25-Jun
1097-0282
Appears in Collections:JOURNAL ARTICLES

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