In this communication we present the peptide-guided assembly of complementary fragments of designed armadillo repeat proteins (dArmRPs) to create proteins that bind peptides not only with high affinity but also with good selectivity. We recently demonstrated that complementary N- and C-terminal fragments of dArmRPs form high-affinity complexes that resemble the structure of the full-length protein, and that these complexes bind their target peptides. We now demonstrate that dArmRPs can be split such that the fragments assemble only in the presence of a templating peptide, and that fragment mixtures enrich the combination with the highest affinity for this peptide. The enriched fragment combination discriminates single amino acid variations in the target peptide with high specificity. Our results suggest novel opportunities for the generation of new peptide binders by selection from dArmRP fragment mixtures.
[NMR paper] Rational design and synthesis of an orally bioavailable peptide guided by NMR amide temperature coefficients.
Rational design and synthesis of an orally bioavailable peptide guided by NMR amide temperature coefficients.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full.gif Related Articles Rational design and synthesis of an orally bioavailable peptide guided by NMR amide temperature coefficients.
Proc Natl Acad Sci U S A. 2014 Dec 9;111(49):17504-9
Authors: Wang CK, Northfield SE, Colless B, Chaousis S, Hamernig I, Lohman RJ, Nielsen DS, Schroeder CI, Liras S, Price...
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[NMR paper] A Combined NMR and Computational Approach to Investigate Peptide Binding to a Designed Armadillo Repeat Protein.
A Combined NMR and Computational Approach to Investigate Peptide Binding to a Designed Armadillo Repeat Protein.
A Combined NMR and Computational Approach to Investigate Peptide Binding to a Designed Armadillo Repeat Protein.
J Mol Biol. 2015 Mar 24;
Authors: Ewald C, Christen MT, Watson RP, Mihajlovic M, Zhou T, Honegger A, Plückthun A, Caflisch A, Zerbe O
Abstract
The specific recognition of peptide sequences by proteins plays an important role both in biology and in diagnostic applications. Here we characterize the...
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A Combined NMR and Computational Approach to Investigate Peptide Binding to a Designed Armadillo Repeat Protein
A Combined NMR and Computational Approach to Investigate Peptide Binding to a Designed Armadillo Repeat Protein
Publication date: Available online 24 March 2015
Source:Journal of Molecular Biology</br>
Author(s): Christina Ewald , Martin T. Christen , Randall P. Watson , Maja Mihajlovic , Ting Zhou , Annemarie Honegger , Andreas Plückthun , Amedeo Caflisch , Oliver Zerbe</br>
The specific recognition of peptide sequences by proteins plays an important role both in biology and in diagnostic applications. Here we characterize the relatively weak binding of the...
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03-25-2015 10:15 AM
Chelation of Ca2+ ions by a peptide from the repeat region of the Plasmodium ... - 7thSpace Interactive (press release)
<img alt="" height="1" width="1" />
Chelation of Ca2+ ions by a peptide from the repeat region of the Plasmodium ...
7thSpace Interactive (press release)
... of Ca2+ by the (NANPNVDP)3NANP peptide, which contains the first seven 4-amino-acid blocks of the repeat region of the P. falciparum circumsporozoite protein, is tested with the use of circular dichroism and nuclear magnetic resonance spectroscopies.
Chelation of Ca2+ ions by a peptide from the repeat region of the Plasmodium ... - 7thSpace Interactive (press release)
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[NMR paper] Conformational properties of peptide fragments homologous to the 106-114 and 106-126
Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study.
Related Articles Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study.
Org Biomol Chem. 2005 Feb 7;3(3):490-7
Authors: Di Natale G, Impellizzeri G, Pappalardo G
Two peptide fragments, corresponding to the amino acid residues 106-126 (PrP) and 106-114 (PrP) of the human prion protein have...
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11-24-2010 10:03 PM
[NMR paper] Reconstitution of a native-like SH2 domain from disordered peptide fragments examined
Reconstitution of a native-like SH2 domain from disordered peptide fragments examined by multidimensional heteronuclear NMR.
Related Articles Reconstitution of a native-like SH2 domain from disordered peptide fragments examined by multidimensional heteronuclear NMR.
Protein Sci. 2001 Nov;10(11):2162-75
Authors: Ojennus DD, Fleissner MR, Wuttke DS
The N-terminal SH2 domain from the p85alpha subunit of phosphatidylinositol 3' kinase is cleaved specifically into 9- and 5-kD fragments by limited proteolytic digestion with trypsin. The noncovalent...
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[NMR paper] Orientation of peptide fragments from Sos proteins bound to the N-terminal SH3 domain
Orientation of peptide fragments from Sos proteins bound to the N-terminal SH3 domain of Grb2 determined by NMR spectroscopy.
Related Articles Orientation of peptide fragments from Sos proteins bound to the N-terminal SH3 domain of Grb2 determined by NMR spectroscopy.
Biochemistry. 1994 Nov 22;33(46):13531-9
Authors: Wittekind M, Mapelli C, Farmer BT, Suen KL, Goldfarb V, Tsao J, Lavoie T, Barbacid M, Meyers CA, Mueller L
NMR spectroscopy has been used to characterize the protein-protein interactions between the mouse Grb2 (mGrb2) N-terminal...
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[NMR paper] 1H NMR analysis of fibril-forming peptide fragments of transthyretin.
1H NMR analysis of fibril-forming peptide fragments of transthyretin.
Related Articles 1H NMR analysis of fibril-forming peptide fragments of transthyretin.
Int J Pept Protein Res. 1994 Oct;44(4):388-98
Authors: Jarvis JA, Kirkpatrick A, Craik DJ
Peptide fragments of the protein transthyretin, previously shown to form cross beta-sheet amyloid-like fibrils in vitro, were investigated using 1H 1D and 2D NMR techniques. TTR 10-20, TTR 105-115 as well as a substituted analogue, (TTR 105-115Met111) all formed amyloid-like fibrils readily in 20-30%...
Peptide-Guided Assembly of Repeat Protein Fragments
Linear Mode
