Modulation of protein-ligand interactions by photocleavage of a cyclic peptide using phosphatidylinositol 3-kinase SH3 domain as model system

Isao Takahashi; Shigeki Kuroiwa; Hanna E. Lindfors; Lionel A. Ndamba; Yoshitaka Hiruma; Tatsuo Yajima; Nobuyuki Okishio; Marcellus Ubbink; Shun Hirota

doi:10.1002/psc.1132

Modulation of protein-ligand interactions by photocleavage of a cyclic peptide using phosphatidylinositol 3-kinase SH3 domain as model system

Isao Takahashi, Shigeki Kuroiwa, Hanna E. Lindfors, Lionel A. Ndamba, Yoshitaka Hiruma, Tatsuo Yajima, Nobuyuki Okishio, Marcellus Ubbink, Shun Hirota^*

^*Corresponding author for this work

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

5 Citations (Scopus)

Abstract

To photomodulate the interaction of the phosphatidylinositol 3-kinase SH3 domain with a peptide ligand, a cyclic peptide (cyclic-1)with a photolabile side chain-to-side chain linkerwas synthesized. The conformation of cyclic-1 differs from that of the parent linear peptide, but becomes identical by UV-irradiation. Accordingly, the binding affinity of cyclic-1 to the SH3 domain increased upon conversion of the cyclic to a linear flexible structure by irradiation (K_d: 3.4 ± 1.7 and 0.9 ± 0.3mM, respectively). These results confirm the usefulness of a photocleavable peptide for photocontrol of peptide-protein interactions.

Original language	English
Pages (from-to)	411-416
Number of pages	6
Journal	Journal of Peptide Science
Volume	15
Issue number	6
DOIs	https://doi.org/10.1002/psc.1132
Publication status	Published - 2009
Externally published	Yes

Keywords

Cyclic peptide
Phosphatidylinositol 3-kinase SH3 domain
Photocleavage
Photomodulation
Protein-peptide interaction
RLP1 peptide

ASJC Scopus subject areas

Structural Biology
Biochemistry
Molecular Medicine
Molecular Biology
Pharmacology
Drug Discovery
Organic Chemistry

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10.1002/psc.1132

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title = "Modulation of protein-ligand interactions by photocleavage of a cyclic peptide using phosphatidylinositol 3-kinase SH3 domain as model system",

abstract = "To photomodulate the interaction of the phosphatidylinositol 3-kinase SH3 domain with a peptide ligand, a cyclic peptide (cyclic-1)with a photolabile side chain-to-side chain linkerwas synthesized. The conformation of cyclic-1 differs from that of the parent linear peptide, but becomes identical by UV-irradiation. Accordingly, the binding affinity of cyclic-1 to the SH3 domain increased upon conversion of the cyclic to a linear flexible structure by irradiation (Kd: 3.4 ± 1.7 and 0.9 ± 0.3mM, respectively). These results confirm the usefulness of a photocleavable peptide for photocontrol of peptide-protein interactions.",

keywords = "Cyclic peptide, Phosphatidylinositol 3-kinase SH3 domain, Photocleavage, Photomodulation, Protein-peptide interaction, RLP1 peptide",

author = "Isao Takahashi and Shigeki Kuroiwa and Lindfors, {Hanna E.} and Ndamba, {Lionel A.} and Yoshitaka Hiruma and Tatsuo Yajima and Nobuyuki Okishio and Marcellus Ubbink and Shun Hirota",

year = "2009",

doi = "10.1002/psc.1132",

language = "English",

volume = "15",

pages = "411--416",

journal = "Journal of Peptide Science",

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TY - JOUR

T1 - Modulation of protein-ligand interactions by photocleavage of a cyclic peptide using phosphatidylinositol 3-kinase SH3 domain as model system

AU - Takahashi, Isao

AU - Kuroiwa, Shigeki

AU - Lindfors, Hanna E.

AU - Ndamba, Lionel A.

AU - Hiruma, Yoshitaka

AU - Yajima, Tatsuo

AU - Okishio, Nobuyuki

AU - Ubbink, Marcellus

AU - Hirota, Shun

PY - 2009

Y1 - 2009

N2 - To photomodulate the interaction of the phosphatidylinositol 3-kinase SH3 domain with a peptide ligand, a cyclic peptide (cyclic-1)with a photolabile side chain-to-side chain linkerwas synthesized. The conformation of cyclic-1 differs from that of the parent linear peptide, but becomes identical by UV-irradiation. Accordingly, the binding affinity of cyclic-1 to the SH3 domain increased upon conversion of the cyclic to a linear flexible structure by irradiation (Kd: 3.4 ± 1.7 and 0.9 ± 0.3mM, respectively). These results confirm the usefulness of a photocleavable peptide for photocontrol of peptide-protein interactions.

AB - To photomodulate the interaction of the phosphatidylinositol 3-kinase SH3 domain with a peptide ligand, a cyclic peptide (cyclic-1)with a photolabile side chain-to-side chain linkerwas synthesized. The conformation of cyclic-1 differs from that of the parent linear peptide, but becomes identical by UV-irradiation. Accordingly, the binding affinity of cyclic-1 to the SH3 domain increased upon conversion of the cyclic to a linear flexible structure by irradiation (Kd: 3.4 ± 1.7 and 0.9 ± 0.3mM, respectively). These results confirm the usefulness of a photocleavable peptide for photocontrol of peptide-protein interactions.

KW - Cyclic peptide

KW - Phosphatidylinositol 3-kinase SH3 domain

KW - Photocleavage

KW - Photomodulation

KW - Protein-peptide interaction

KW - RLP1 peptide

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Modulation of protein-ligand interactions by photocleavage of a cyclic peptide using phosphatidylinositol 3-kinase SH3 domain as model system

Abstract

Keywords

ASJC Scopus subject areas

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