Exploring the possible binding sites at the interface of triosephosphate isomerase dimer as a potential target for anti-tripanosomal drug design

L. Michel Espinoza-Fonseca; José G. Trujillo-Ferrara

doi:10.1016/j.bmcl.2004.04.013

Exploring the possible binding sites at the interface of triosephosphate isomerase dimer as a potential target for anti-tripanosomal drug design

L. Michel Espinoza-Fonseca
, José G. Trujillo-Ferrara

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

21 Scopus citations

Abstract

To explore the possible binding sites at the interface of tripanosomal triosephosphate isomerase, fully flexible benzothiazoles were docked onto the dimer interface. Docking studies revealed that the most favorable interactions occur in the aromatic clusters of the dimeric form. Hence is purposed that the dimer disruption is not via Cys 15, as presented in last studies, but it could be carried out through the unstabilization of π-π interactions of two aromatic clusters present in the interface. These studies enable a novel alternative for rational structure-based anti-tripanosomal drug design.

Original language	English (US)
Pages (from-to)	3151-3154
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	14
Issue number	12
DOIs	https://doi.org/10.1016/j.bmcl.2004.04.013
State	Published - Jun 21 2004
Externally published	Yes

Bibliographical note

Funding Information:
We thank Drs. Armando Gómez-Puyou, Ruy Pérez-Montfort and Arturo Rojo-Dominguez for fruitful discussions about this work. This work was supported under CONACYT and CGPI-IPN grants 31935 and 200860.

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10.1016/j.bmcl.2004.04.013

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abstract = "To explore the possible binding sites at the interface of tripanosomal triosephosphate isomerase, fully flexible benzothiazoles were docked onto the dimer interface. Docking studies revealed that the most favorable interactions occur in the aromatic clusters of the dimeric form. Hence is purposed that the dimer disruption is not via Cys 15, as presented in last studies, but it could be carried out through the unstabilization of π-π interactions of two aromatic clusters present in the interface. These studies enable a novel alternative for rational structure-based anti-tripanosomal drug design.",

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Exploring the possible binding sites at the interface of triosephosphate isomerase dimer as a potential target for anti-tripanosomal drug design

Abstract

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