De novo protein surface design: Use of cation-π interactions to enhance binding between an α-helical peptide and a cationic molecule in 50% aqueous solution

Brendan P. Orner; Xavier Salvatella; Jorge Sánchez Quesada; Javier De Mendoza; Ernest Giralt; Andrew D. Hamilton

doi:10.1002/1521-3773(20020104)41:1<117::AID-ANIE117>3.0.CO;2-J

De novo protein surface design: Use of cation-π interactions to enhance binding between an α-helical peptide and a cationic molecule in 50% aqueous solution

Brendan P. Orner, Xavier Salvatella, Jorge Sánchez Quesada, Javier De Mendoza, Ernest Giralt, Andrew D. Hamilton

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

The relative position of the Asp and Trp residues in a peptide chain is important for recognizing a tetraguanidinium receptor through hydrogen bonding and cation-π interactions. The molecule not only binds with high affinity (K_a = 1.1 x 10⁸M^-1), it also stabilizes the helical schematic representation) as demonstrated by NMR and CD spectroscopy.

Original language	English (US)
Pages (from-to)	117-119
Number of pages	3
Journal	Angewandte Chemie - International Edition
Volume	41
Issue number	1
DOIs	https://doi.org/10.1002/1521-3773(20020104)41:1<117::AID-ANIE117>3.0.CO;2-J
State	Published - Jan 4 2002

Keywords

Helical structures
Host-guest systems
Molecular recognition
NMR spectroscopy
Noncovalent interactions

ASJC Scopus subject areas

Catalysis
Chemistry(all)

Access to Document

10.1002/1521-3773(20020104)41:1<117::AID-ANIE117>3.0.CO;2-J

Cite this

Orner, B. P., Salvatella, X., Sánchez Quesada, J., De Mendoza, J., Giralt, E., & Hamilton, A. D. (2002). De novo protein surface design: Use of cation-π interactions to enhance binding between an α-helical peptide and a cationic molecule in 50% aqueous solution. Angewandte Chemie - International Edition, 41(1), 117-119. https://doi.org/10.1002/1521-3773(20020104)41:1<117::AID-ANIE117>3.0.CO;2-J

De novo protein surface design : Use of cation-π interactions to enhance binding between an α-helical peptide and a cationic molecule in 50% aqueous solution. / Orner, Brendan P.; Salvatella, Xavier; Sánchez Quesada, Jorge; De Mendoza, Javier; Giralt, Ernest; Hamilton, Andrew D.

In: Angewandte Chemie - International Edition, Vol. 41, No. 1, 04.01.2002, p. 117-119.

Research output: Contribution to journal › Article › peer-review

Orner, BP, Salvatella, X, Sánchez Quesada, J, De Mendoza, J, Giralt, E & Hamilton, AD 2002, 'De novo protein surface design: Use of cation-π interactions to enhance binding between an α-helical peptide and a cationic molecule in 50% aqueous solution', Angewandte Chemie - International Edition, vol. 41, no. 1, pp. 117-119. https://doi.org/10.1002/1521-3773(20020104)41:1<117::AID-ANIE117>3.0.CO;2-J

Orner BP, Salvatella X, Sánchez Quesada J, De Mendoza J, Giralt E, Hamilton AD. De novo protein surface design: Use of cation-π interactions to enhance binding between an α-helical peptide and a cationic molecule in 50% aqueous solution. Angewandte Chemie - International Edition. 2002 Jan 4;41(1):117-119. https://doi.org/10.1002/1521-3773(20020104)41:1<117::AID-ANIE117>3.0.CO;2-J

Orner, Brendan P. ; Salvatella, Xavier ; Sánchez Quesada, Jorge ; De Mendoza, Javier ; Giralt, Ernest ; Hamilton, Andrew D. / De novo protein surface design : Use of cation-π interactions to enhance binding between an α-helical peptide and a cationic molecule in 50% aqueous solution. In: Angewandte Chemie - International Edition. 2002 ; Vol. 41, No. 1. pp. 117-119.

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abstract = "The relative position of the Asp and Trp residues in a peptide chain is important for recognizing a tetraguanidinium receptor through hydrogen bonding and cation-π interactions. The molecule not only binds with high affinity (Ka = 1.1 x 108M-1), it also stabilizes the helical schematic representation) as demonstrated by NMR and CD spectroscopy.",

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De novo protein surface design: Use of cation-π interactions to enhance binding between an α-helical peptide and a cationic molecule in 50% aqueous solution

Abstract

Keywords

ASJC Scopus subject areas

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