Huck Bayard R, Fisk John D, Guzei Ilia A, Carlson Heather A, Gellman Samuel H
Department of Chemistry and Graduate Program in Biophysics, University of Wisconsin, Madison, WI 53706, USA.
J Am Chem Soc. 2003 Jul 30;125(30):9035-7. doi: 10.1021/ja034561c.
We examine a new class of beta-peptides, 2,2-disubstituted pyrrolidine-4-carboxylic acid oligomers, and show that they manifest discrete conformational preferences despite the impossibility of internal hydrogen bonding. Numerous beta-peptide families have been described that display specific secondary structural preferences, but all of the conformations characterized in detail so far have contained internal hydrogen bonds. Internal hydrogen bonding is observed within the most common secondary structures of conventional peptides as well. Identifying foldamers in which shape control is independent of hydrogen bonding is significant in two ways. At a fundamental level, foldamers in this small but growing class are interesting because their shapes are controlled by distinctive networks of noncovalent forces. At a practical level, non-hydrogen bonded foldamers may be useful in biomedical applications because the low intrinsic polarity of their backbones may promote bioavailability.
我们研究了一类新型的β-肽，即2,2-二取代吡咯烷-4-羧酸低聚物，并表明尽管它们无法形成分子内氢键，但仍表现出离散的构象偏好。已经描述了许多显示特定二级结构偏好的β-肽家族，但迄今为止详细表征的所有构象都包含分子内氢键。在传统肽的最常见二级结构中也观察到分子内氢键。识别形状控制独立于氢键的折叠体在两个方面具有重要意义。在基础层面上，这类规模虽小但不断增长的折叠体很有趣，因为它们的形状由独特的非共价力网络控制。在实际层面上，非氢键结合的折叠体可能在生物医学应用中有用，因为其主链的低固有极性可能促进生物利用度。
