Identification of GDF15 peptide fragments inhibiting GFRAL receptor signaling

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

Standard

Identification of GDF15 peptide fragments inhibiting GFRAL receptor signaling. / Alexopoulou, Flora; Buch-Månson, Nina; Pedersen, Søren Ljungberg; Vrang, Niels; Fink, Lisbeth Nielsen; Strømgaard, Kristian.

In: Peptides, Vol. 168, 171063, 2023.

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

Harvard

Alexopoulou, F, Buch-Månson, N, Pedersen, SL, Vrang, N, Fink, LN & Strømgaard, K 2023, 'Identification of GDF15 peptide fragments inhibiting GFRAL receptor signaling', Peptides, vol. 168, 171063. https://doi.org/10.1016/j.peptides.2023.171063

APA

Alexopoulou, F., Buch-Månson, N., Pedersen, S. L., Vrang, N., Fink, L. N., & Strømgaard, K. (2023). Identification of GDF15 peptide fragments inhibiting GFRAL receptor signaling. Peptides, 168, [171063]. https://doi.org/10.1016/j.peptides.2023.171063

Vancouver

Alexopoulou F, Buch-Månson N, Pedersen SL, Vrang N, Fink LN, Strømgaard K. Identification of GDF15 peptide fragments inhibiting GFRAL receptor signaling. Peptides. 2023;168. 171063. https://doi.org/10.1016/j.peptides.2023.171063

Author

Alexopoulou, Flora ; Buch-Månson, Nina ; Pedersen, Søren Ljungberg ; Vrang, Niels ; Fink, Lisbeth Nielsen ; Strømgaard, Kristian. / Identification of GDF15 peptide fragments inhibiting GFRAL receptor signaling. In: Peptides. 2023 ; Vol. 168.

Bibtex

@article{f576f92b35014e4bb2d487acd96d8013,

title = "Identification of GDF15 peptide fragments inhibiting GFRAL receptor signaling",

abstract = "Growth differentiation factor 15 (GDF15) is believed to be a major causative factor for cancer-induced cachexia. Recent elucidation of the central circuits involved in GDF15 function and its signaling through the glial cell-derived neurotrophic factor family receptor α-like (GFRAL) has prompted the interest of targeting the GDF15-GFRAL signaling for energy homeostasis and body weight regulation. Here, we applied advanced peptide technologies to identify GDF15 peptide fragments inhibiting GFRAL signaling. SPOT peptide arrays revealed binding of GDF15 C-terminal peptide fragments to the extracellular domain of GFRAL. Parallel solid-phase peptide synthesis allowed for generation of complementary GDF15 peptide libraries and their subsequent functional evaluation in cells expressing the GFRAL/RET receptor complex. We identified a series of C-terminal fragments of GDF15 inhibiting GFRAL activity in the micromolar range. These novel GFRAL peptide inhibitors could serve as valuable tools for further development of peptide therapeutics towards the treatment of cachexia and other wasting disorders.",

keywords = "Cachexia, GDF15, GFRAL, Peptide inhibitors, Peptide technologies",

author = "Flora Alexopoulou and Nina Buch-M{\aa}nson and Pedersen, {S{\o}ren Ljungberg} and Niels Vrang and Fink, {Lisbeth Nielsen} and Kristian Str{\o}mgaard",

note = "Publisher Copyright: {\textcopyright} 2023 The Authors",

year = "2023",

doi = "10.1016/j.peptides.2023.171063",

language = "English",

volume = "168",

journal = "Peptides",

issn = "0196-9781",

publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Identification of GDF15 peptide fragments inhibiting GFRAL receptor signaling

AU - Alexopoulou, Flora

AU - Buch-Månson, Nina

AU - Pedersen, Søren Ljungberg

AU - Vrang, Niels

AU - Fink, Lisbeth Nielsen

AU - Strømgaard, Kristian

PY - 2023

Y1 - 2023

N2 - Growth differentiation factor 15 (GDF15) is believed to be a major causative factor for cancer-induced cachexia. Recent elucidation of the central circuits involved in GDF15 function and its signaling through the glial cell-derived neurotrophic factor family receptor α-like (GFRAL) has prompted the interest of targeting the GDF15-GFRAL signaling for energy homeostasis and body weight regulation. Here, we applied advanced peptide technologies to identify GDF15 peptide fragments inhibiting GFRAL signaling. SPOT peptide arrays revealed binding of GDF15 C-terminal peptide fragments to the extracellular domain of GFRAL. Parallel solid-phase peptide synthesis allowed for generation of complementary GDF15 peptide libraries and their subsequent functional evaluation in cells expressing the GFRAL/RET receptor complex. We identified a series of C-terminal fragments of GDF15 inhibiting GFRAL activity in the micromolar range. These novel GFRAL peptide inhibitors could serve as valuable tools for further development of peptide therapeutics towards the treatment of cachexia and other wasting disorders.

AB - Growth differentiation factor 15 (GDF15) is believed to be a major causative factor for cancer-induced cachexia. Recent elucidation of the central circuits involved in GDF15 function and its signaling through the glial cell-derived neurotrophic factor family receptor α-like (GFRAL) has prompted the interest of targeting the GDF15-GFRAL signaling for energy homeostasis and body weight regulation. Here, we applied advanced peptide technologies to identify GDF15 peptide fragments inhibiting GFRAL signaling. SPOT peptide arrays revealed binding of GDF15 C-terminal peptide fragments to the extracellular domain of GFRAL. Parallel solid-phase peptide synthesis allowed for generation of complementary GDF15 peptide libraries and their subsequent functional evaluation in cells expressing the GFRAL/RET receptor complex. We identified a series of C-terminal fragments of GDF15 inhibiting GFRAL activity in the micromolar range. These novel GFRAL peptide inhibitors could serve as valuable tools for further development of peptide therapeutics towards the treatment of cachexia and other wasting disorders.

KW - Cachexia

KW - GDF15

KW - GFRAL

KW - Peptide inhibitors

KW - Peptide technologies

U2 - 10.1016/j.peptides.2023.171063

DO - 10.1016/j.peptides.2023.171063

M3 - Journal article

C2 - 37495041

AN - SCOPUS:85166287258

VL - 168

JO - Peptides

JF - Peptides

SN - 0196-9781

M1 - 171063

ER -

ID: 366507258