Biophysical characterization of the proton-coupled oligopeptide transporter YjdL

Department of Drug Design and Pharmacology

Biophysical characterization of the proton-coupled oligopeptide transporter YjdL

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Biophysical characterization of the proton-coupled oligopeptide transporter YjdL. / Jensen, Johanne Mørch; Simonsen, Fie C.; Mastali, Amir; Hald, Helle; Lillebro, Ida; Diness, Frederik; Olsen, Lars; Mirza, Osman Asghar.

In: Peptides, Vol. 38, No. 1, 11.2012, p. 89-93.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Jensen, JM, Simonsen, FC, Mastali, A, Hald, H, Lillebro, I, Diness, F, Olsen, L & Mirza, OA 2012, 'Biophysical characterization of the proton-coupled oligopeptide transporter YjdL', Peptides, vol. 38, no. 1, pp. 89-93. https://doi.org/10.1016/j.peptides.2012.08.012

APA

Jensen, J. M., Simonsen, F. C., Mastali, A., Hald, H., Lillebro, I., Diness, F., Olsen, L., & Mirza, O. A. (2012). Biophysical characterization of the proton-coupled oligopeptide transporter YjdL. Peptides, 38(1), 89-93. https://doi.org/10.1016/j.peptides.2012.08.012

Vancouver

Jensen JM, Simonsen FC, Mastali A, Hald H, Lillebro I, Diness F et al. Biophysical characterization of the proton-coupled oligopeptide transporter YjdL. Peptides. 2012 Nov;38(1):89-93. https://doi.org/10.1016/j.peptides.2012.08.012

Author

Jensen, Johanne Mørch ; Simonsen, Fie C. ; Mastali, Amir ; Hald, Helle ; Lillebro, Ida ; Diness, Frederik ; Olsen, Lars ; Mirza, Osman Asghar. / Biophysical characterization of the proton-coupled oligopeptide transporter YjdL. In: Peptides. 2012 ; Vol. 38, No. 1. pp. 89-93.

Bibtex

@article{8263798046f34ba39579c01f50990fc2,

title = "Biophysical characterization of the proton-coupled oligopeptide transporter YjdL",

abstract = "Proton-coupled oligopeptide transporters (POTs) utilize the electrochemical proton gradient to facilitate uptake of di- or tripeptide molecules. YjdL is one of four POTs found in Escherichia coli. It has shown an extraordinary preference for di- rather than tripeptides, and is therefore significantly different from prototypical POTs such as the human hPepT1. Nonetheless YjdL contains several highly conserved POT residues, which include Glu388 that is located in the putative substrate binding cavity. Here we present biophysical characterization of WT-YjdL and Glu388Gln. Isothermal titration calorimetrical studies exhibit a K(d) of 14 µM for binding of Ala-Lys to WT-YjdL. Expectedly, no binding could be detected for the tripeptide Ala-Ala-Lys. Surprisingly however, binding could not be detected for Ala-Gln, although earlier studies indicated inhibitory potencies of Ala-Gln to be comparable to Ala-Lys (IC(50) values of 0.6 compared to 0.3mM). Finally, Ala-Lys binding to Glu388Gln was also undetectable which may support a previously suggested role in interaction with the ligand peptide N-terminus.",

author = "Jensen, {Johanne M{\o}rch} and Simonsen, {Fie C.} and Amir Mastali and Helle Hald and Ida Lillebro and Frederik Diness and Lars Olsen and Mirza, {Osman Asghar}",

year = "2012",

month = nov,

doi = "10.1016/j.peptides.2012.08.012",

language = "English",

volume = "38",

pages = "89--93",

journal = "Peptides",

issn = "0196-9781",

publisher = "Elsevier",

number = "1",

}

RIS

TY - JOUR

T1 - Biophysical characterization of the proton-coupled oligopeptide transporter YjdL

AU - Jensen, Johanne Mørch

AU - Simonsen, Fie C.

AU - Mastali, Amir

AU - Hald, Helle

AU - Lillebro, Ida

AU - Diness, Frederik

AU - Olsen, Lars

AU - Mirza, Osman Asghar

PY - 2012/11

Y1 - 2012/11

N2 - Proton-coupled oligopeptide transporters (POTs) utilize the electrochemical proton gradient to facilitate uptake of di- or tripeptide molecules. YjdL is one of four POTs found in Escherichia coli. It has shown an extraordinary preference for di- rather than tripeptides, and is therefore significantly different from prototypical POTs such as the human hPepT1. Nonetheless YjdL contains several highly conserved POT residues, which include Glu388 that is located in the putative substrate binding cavity. Here we present biophysical characterization of WT-YjdL and Glu388Gln. Isothermal titration calorimetrical studies exhibit a K(d) of 14 µM for binding of Ala-Lys to WT-YjdL. Expectedly, no binding could be detected for the tripeptide Ala-Ala-Lys. Surprisingly however, binding could not be detected for Ala-Gln, although earlier studies indicated inhibitory potencies of Ala-Gln to be comparable to Ala-Lys (IC(50) values of 0.6 compared to 0.3mM). Finally, Ala-Lys binding to Glu388Gln was also undetectable which may support a previously suggested role in interaction with the ligand peptide N-terminus.

AB - Proton-coupled oligopeptide transporters (POTs) utilize the electrochemical proton gradient to facilitate uptake of di- or tripeptide molecules. YjdL is one of four POTs found in Escherichia coli. It has shown an extraordinary preference for di- rather than tripeptides, and is therefore significantly different from prototypical POTs such as the human hPepT1. Nonetheless YjdL contains several highly conserved POT residues, which include Glu388 that is located in the putative substrate binding cavity. Here we present biophysical characterization of WT-YjdL and Glu388Gln. Isothermal titration calorimetrical studies exhibit a K(d) of 14 µM for binding of Ala-Lys to WT-YjdL. Expectedly, no binding could be detected for the tripeptide Ala-Ala-Lys. Surprisingly however, binding could not be detected for Ala-Gln, although earlier studies indicated inhibitory potencies of Ala-Gln to be comparable to Ala-Lys (IC(50) values of 0.6 compared to 0.3mM). Finally, Ala-Lys binding to Glu388Gln was also undetectable which may support a previously suggested role in interaction with the ligand peptide N-terminus.

U2 - 10.1016/j.peptides.2012.08.012

DO - 10.1016/j.peptides.2012.08.012

M3 - Journal article

C2 - 22940668

VL - 38

SP - 89

EP - 93

JO - Peptides

JF - Peptides

SN - 0196-9781

IS - 1

ER -

ID: 44863840