Conformational properties of β-residue-containing oligopeptides in apolar solvent

被引：5

作者：

Aschi, M

Mollica, A

Lucente, G

Paradisi, MP

Mazza, F

机构：

[1] Univ Aquila, Dipartimento Chim Ingn Chim & Mat, I-67100 Laquila, Italy

[2] Univ Roma La Sapienza, Sez Roma, CNR, Dipartimento Studi Farmaceut, Rome, Italy

[3] Univ Roma La Sapienza, Sez Roma, CNR, Ist Chim Biomol, Rome, Italy

来源：

JOURNAL OF MOLECULAR STRUCTURE | 2006年 / 785卷 / 1-3期

关键词：

beta-aminoacids; conformational analysis; molecular dynamics; peptides; 1H NMR;

D O I：

10.1016/j.molstruc.2005.10.009

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Molecular dynamics simulations carried out on short linear peptides incorporating P-Ala residues, namely Boc-beta-Ala-Phe-OMe (1) and Boc-Met-beta-Ala-Phe-OMe (2), reveal a markedly different conformational-dynamical behaviour. The tripeptide (2), showing free energy minima deeper than the dipeptide is predicted to be characterized by long-lived conformers. The present theoretical results may help in rationalizing experimental (IR, NMR) results on (1) and (2) and definitely show the importance of a dynamical approach for a correct interpretation and prediction of the conformational behaviour in solution even for relatively small molecules. (c) 2005 Elsevier B.V. All rights reserved.

引用

页码：176 / 181

页数：6