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Conformational Profile of a Proline−Arginine Hybrid

AutorRevilla-López, G.; Jiménez, Ana I. ; Cativiela, Carlos ; Nussinov, Ruth; Alemán, Carlos; Zanuy, David
Fecha de publicación2010
EditorAmerican Chemical Society
CitaciónJournal of Chemical Information and Modeling 50(10): 1781-1789 (2010)
ResumenThe intrinsic conformational preferences of a new nonproteinogenic amino acid have been explored by computational methods. This tailored molecule, named (βPro)Arg, is conceived as a replacement for arginine in bioactive peptides when the stabilization of folded turn-like conformations is required. The new residue features a proline skeleton that bears the guanidilated side chain of arginine at the Cβ position of the five-membered pyrrolidine ring, in either a cis or a trans orientation with respect to the carboxylic acid. The conformational profiles of the N-acetyl-N′-methylamide derivatives of the cis and trans isomers of (βPro)Arg have been examined in the gas phase and in solution by B3LYP/6-31+G(d,p) calculations and molecular dynamics simulations. The main conformational features of both isomers represent a balance between geometric restrictions imposed by the five-membered pyrrolidine ring and the ability of the guanidilated side chain to interact with the backbone through hydrogen bonds. Thus, both cis- and trans-(βPro)Arg exhibit a preference for the αL conformation as a consequence of the interactions established between the guanidinium moiety and the main-chain amide groups.
Identificadoresdoi: 10.1021/ci100135f
issn: 1549-9596
e-issn: 1549-960X
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