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首页> 外文期刊>Bioorganic and Medicinal Chemistry Letters >In vitro stability of alpha-Helical peptide nucleic acids (alphaPNAs).
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In vitro stability of alpha-Helical peptide nucleic acids (alphaPNAs).

机译:α-螺旋肽核酸(alphaPNAs)的体外稳定性。

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摘要

alpha-Helical peptide nucleic acids (alphaPNAs) are synthetic molecules that merge the alpha-helix secondary structure of peptides with the codified Watson-Crick base pairing capability of nucleic acids. It is now demonstrated that alphaPNAs made up of either L- or D-amino acids are resistant to degradation by the proteases present in human serum. The increased stability of alphaPNAs towards proteases may be attributable to the presence of unnatural nucleoamino acid residues [-NHCH(CH(2)OCH(2)B)CO-, where B=thymine or cytosine] since the replacement of these amino acids by serine yields a control peptide that does break down in human serum. The stability of alphaPNAs towards proteases makes them attractive candidates for further development as antisense agents.
机译:α-螺旋肽核酸(alphaPNAs)是将肽的α-螺旋二级结构与核酸的编码Watson-Crick碱基配对能力融合在一起的合成分子。现在证明,由L-或D-氨基酸组成的αPNA对人血清中存在的蛋白酶具有抗降解性。 alphaPNA对蛋白酶的稳定性提高可能归因于存在非天然核苷酸残基[-NHCH(CH(2)OCH(2)B)CO-,其中B =胸腺嘧啶或胞嘧啶],因为这些氨基酸被丝氨酸产生确实在人血清中分解的对照肽。 αPNA对蛋白酶的稳定性使其成为反义剂进一步开发的有吸引力的候选对象。

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