新型螺旋折叠物：1:1α/核苷衍生β-氨基酸序列中组织的杂化主链折叠。
Novel helical foldamers: organized heterogeneous backbone folding in 1 : 1 alpha/nucleoside-derived-beta-amino acid sequences.
机构信息
Organic Division-I, Indian Institute of Chemical Technology (CSIR), Uppal Road, Tarnaka, Hyderabad-500 607 (AP), India.
出版信息
Chem Commun (Camb). 2010 Oct 7;46(37):6962-4. doi: 10.1039/c0cc01724h. Epub 2010 Aug 23.
PMID:20733989
Abstract
Secondary structural conformation of hybrid oligo-peptides comprised of 1 : 1 alternating Nucleoside Derived beta-Amino acid (NDA) and l-amino acid residues has been reported. The studies reveal that the NDA residues organize the heterogeneous backbone featuring the surface properties of both nucleic acids and peptides, to adopt a novel 11/8-helical fold.
摘要
已有报道称，由 1:1 交替核碱基衍生的β-氨基酸（NDA）和 l-氨基酸残基组成的杂合寡肽具有二级结构构象。研究表明，NDA 残基组织了异构骨架，具有核酸和肽的表面特性，以采用一种新的 11/8-螺旋折叠。
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