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• W2071609487 endingPage "3931" @default.
• W2071609487 startingPage "3921" @default.
• W2071609487 abstract "Cyclic peptides with a linear tail (CPLT) have been successfully used to model two zinc fingers (ZFs) adopting the treble-clef- and loosened zinc-ribbon folds. In this article, we examine the factors that may influence the design of such ZF models: mutations in the sequence, size of the cycle, and size of the tail. For this purpose, several peptides derived from the CPLT-based models of the treble-clef- and loosened zinc-ribbon ZF were synthesized and studied. CPLT-based models appear to be robust toward mutations, accommodate various cycle sizes, and are sensible to the size of the linking region of the tail located between the cycle and the coordinating amino acids. Based on these criteria, we describe the design of a new CPLT-based model for the zinc-ribbon ZFs, LZR , and compare it to a linear analogue, LZR(lin) . The model complex Zn⋅LZR is able to fold correctly around the metal ion contrary to Zn⋅LZR(lin) , suggesting that CPLT-based models are more likely to yield structurally meaningful models of ZF sites than linear peptide models. Finally, we draw some rules that could allow the design of new CPLT-based metallopeptides with a controlled fold." @default.
• W2071609487 created "2016-06-24" @default.
• W2071609487 creator A5022678284 @default.
• W2071609487 creator A5033445786 @default.
• W2071609487 creator A5073421573 @default.
• W2071609487 creator A5082105691 @default.
• W2071609487 creator A5088730507 @default.
• W2071609487 date "2013-02-21" @default.
• W2071609487 modified "2023-10-16" @default.
• W2071609487 title "On the Design of Zinc-Finger Models with Cyclic Peptides Bearing a Linear Tail" @default.
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• W2071609487 doi "https://doi.org/10.1002/chem.201204167" @default.
• W2071609487 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23436718" @default.
• W2071609487 hasPublicationYear "2013" @default.
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