A Non‐coded β <sup>2,2</sup> ‐Amino Acid with Isoxazoline Core Able to Stabilize Peptides Folding through an Unprecedented Hydrogen Bond
نویسندگان
چکیده
New peptidomimetics containing a β2,2-isoxazoline amino acid, 5-(aminomethyl)-3-phenyl-4,5-dihydroisoxazole-5-carboxylic acid (Isox-β2,2AA), were prepared and studied by NMR theoretical calculations. Interestingly, inserting R-Isox-β2,2AA in short tri- hexapeptide models, an unexpected α-turn-like motif was observed, thanks to unprecedented strong H-bond involving C=N of isoxazoline side chain β2,2AA.
منابع مشابه
Helical folding of α/β-peptides containing β-amino acids with an eight-membered ring constraint.
αβα-Tripeptide that contains a cyclic β-amino acid with an eight-membered ring, a cis-2-aminocyclooct-5-enecarboxylic acid (cis-ACOE) or a cis-2-aminocyclooctanecarboxylic acid (cis-ACOC) displayed an 11/9-helical turn in the crystal state. The related α/β-peptide oligomers were shown to adopt 11/9-helical conformations in solution.
متن کاملHydrogen Bond Strengths in Phosphorylated and Sulfated Amino Acid Residues
Post-translational modification by the addition of an oxoanion functional group, usually a phosphate group and less commonly a sulfate group, leads to diverse structural and functional consequences in protein systems. Building upon previous studies of the phosphoserine residue (pSer), we address the distinct nature of hydrogen bonding interactions in phosphotyrosine (pTyr) and sulfotyrosine (sT...
متن کاملAn amino acid code for protein folding.
Direct structural information obtained for many proteins supports the following conclusions. The amino acid sequences of proteins can stabilize not only the final native state but also a small set of discrete partially folded native-like intermediates. Intermediates are formed in steps that use as units the cooperative secondary structural elements of the native protein. Earlier intermediates g...
متن کاملMolecular dynamics simulations of peptides containing an unnatural amino acid: dimerization, folding, and protein binding.
We have performed molecular dynamics (MD) simulations to study the dimerization, folding, and binding to a protein of peptides containing an unnatural amino acid. NMR studies have shown that the substitution of one residue in a tripeptide beta-strand by the unnatural amino acid Hao (5-HO2CCONH-2-MeO-C6H3-CO-NHNH2) modifies the conformational flexibility of the beta-strand and the hydrogen-bondi...
متن کاملA study of aromatic hydrogen bonds of peptides with aromatic amino acid side-chains.
The importance of hydrogen bonding studies lies in their structural, biological and medicinal applications. Non-conventional hydrogen bonds are weak, but are found to play an important role in biological molecules. In view of their importance,a study of the aromatic hydrogen bonds in peptides with aromatic amino acid side chains was carried out. The results indicate a reasonable probability for...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: European Journal of Organic Chemistry
سال: 2022
ISSN: ['1434-193X', '1099-0690']
DOI: https://doi.org/10.1002/ejoc.202200601