A rationally designed oligopeptide shows significant conformational changes upon binding to sulphate ions

Demuth, Caspar; Zerbe, Oliver; Rognan, Didier; Söll, Richard; Beck-Sickinger, Annette; Folkers, Gerd; Spichiger, Ursula E.

doi:10.1016/S0956-5663(01)00221-4

Publication type:	Article in scientific journal
Type of review:	Peer review (publication)
Title:	A rationally designed oligopeptide shows significant conformational changes upon binding to sulphate ions
Authors:	Demuth, Caspar Zerbe, Oliver Rognan, Didier Söll, Richard Beck-Sickinger, Annette Folkers, Gerd Spichiger, Ursula E.
DOI:	10.1016/S0956-5663(01)00221-4
Published in:	Biosensors and Bioelectronics
Volume(Issue):	16
Issue:	9-12
Page(s):	783
Pages to:	789
Issue Date:	2001
Publisher / Ed. Institution:	Elsevier
ISSN:	0956-5663 1873-4235
Language:	English
Subject (DDC):	540: Chemistry
Abstract:	Oligopeptides that interact with oxoanions were developed by rational design methods. The substrate-binding site of the enzyme purine nucleoside phosphorylase served as a model for the design of the ionophores. The amino acids involved in the complexation of oxoanions were linked through flexible spacer residues. These spacers were chosen such that the relative orientation of the interacting amino acids was conserved. Several peptide sequences were preselected based on intermolecular H-bond frequencies. These frequencies were calculated from molecular dynamics trajectories of the corresponding peptide-anion complexes and used to score the binding properties of the peptides. The most promising peptides were prepared using solid phase peptide synthesis. Anion binding of the peptide ionophores was screened using circular dichroism (CD) and confirmed by NMR spectroscopy. CD measurements performed in methanol revealed a significant conformational change of a linear undecapeptide upon binding to sulphate ions. Two-dimensional-NMR experiments confirmed that a conformation with high helical content is formed in the presence of sulphate ions. These conformational changes induced by the anion stimulate the development of new transduction mechanisms in chemical sensors.
URI:	https://digitalcollection.zhaw.ch/handle/11475/14536
Fulltext version:	Published version
License (according to publishing contract):	Licence according to publishing contract
Departement:	Life Sciences and Facility Management
Organisational Unit:	Institute of Chemistry and Biotechnology (ICBT)
Appears in collections:	Publikationen Life Sciences und Facility Management

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Demuth, C., Zerbe, O., Rognan, D., Söll, R., Beck-Sickinger, A., Folkers, G., & Spichiger, U. E. (2001). A rationally designed oligopeptide shows significant conformational changes upon binding to sulphate ions. Biosensors and Bioelectronics, 16(9-12), 783–789. https://doi.org/10.1016/S0956-5663(01)00221-4

Demuth, C. et al. (2001) ‘A rationally designed oligopeptide shows significant conformational changes upon binding to sulphate ions’, Biosensors and Bioelectronics, 16(9-12), pp. 783–789. Available at: https://doi.org/10.1016/S0956-5663(01)00221-4.

C. Demuth et al., “A rationally designed oligopeptide shows significant conformational changes upon binding to sulphate ions,” Biosensors and Bioelectronics, vol. 16, no. 9-12, pp. 783–789, 2001, doi: 10.1016/S0956-5663(01)00221-4.

DEMUTH, Caspar, Oliver ZERBE, Didier ROGNAN, Richard SÖLL, Annette BECK-SICKINGER, Gerd FOLKERS und Ursula E. SPICHIGER, 2001. A rationally designed oligopeptide shows significant conformational changes upon binding to sulphate ions. Biosensors and Bioelectronics. 2001. Bd. 16, Nr. 9-12, S. 783–789. DOI 10.1016/S0956-5663(01)00221-4

Demuth, Caspar, Oliver Zerbe, Didier Rognan, Richard Söll, Annette Beck-Sickinger, Gerd Folkers, and Ursula E. Spichiger. 2001. “A Rationally Designed Oligopeptide Shows Significant Conformational Changes upon Binding to Sulphate Ions.” Biosensors and Bioelectronics 16 (9-12): 783–89. https://doi.org/10.1016/S0956-5663(01)00221-4.

Demuth, Caspar, et al. “A Rationally Designed Oligopeptide Shows Significant Conformational Changes upon Binding to Sulphate Ions.” Biosensors and Bioelectronics, vol. 16, no. 9-12, 2001, pp. 783–89, https://doi.org/10.1016/S0956-5663(01)00221-4.