Development of cyclic peptides with potent in vivo osteogenic activity through RaPID-based affinity maturation.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
08 12 2020
Historique:
pubmed: 25 11 2020
medline: 22 1 2021
entrez: 24 11 2020
Statut: ppublish

Résumé

Osteoporosis is caused by a disequilibrium between bone resorption and bone formation. Therapeutics for osteoporosis can be divided into antiresorptives that suppress bone resorption and anabolics which increase bone formation. Currently, the only anabolic treatment options are parathyroid hormone mimetics or an anti-sclerostin monoclonal antibody. With the current global increases in demographics at risk for osteoporosis, development of therapeutics that elicit anabolic activity through alternative mechanisms is imperative. Blockade of the PlexinB1 and Semaphorin4D interaction on osteoblasts has been shown to be a promising mechanism to increase bone formation. Here we report the discovery of cyclic peptides by a novel RaPID (Random nonstandard Peptides Integrated Discovery) system-based affinity maturation methodology that generated the peptide PB1m6A9 which binds with high affinity to both human and mouse PlexinB1. The chemically dimerized peptide, PB1

Identifiants

pubmed: 33229551
pii: 2012266117
doi: 10.1073/pnas.2012266117
pmc: PMC7733813
doi:

Substances chimiques

Peptide Library 0
Peptides, Cyclic 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

31070-31077

Informations de copyright

Copyright © 2020 the Author(s). Published by PNAS.

Déclaration de conflit d'intérêts

Competing interest statement: N.K.B., Y.M., J.T., and H.S. are inventors of a patent application titled “Plexin Binding Regulator” (US20190247457A1). All other authors declare no competing interests.

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Auteurs

Nasir K Bashiruddin (NK)

Department of Chemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033 Japan.

Mikihito Hayashi (M)

Department of Cell Signaling, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University, Tokyo 113-8549, Japan.
Japan Agency for Medical Research and Development, Precursory Research for Innovative Medical Care, Tokyo 113-8549, Japan.

Masanobu Nagano (M)

Department of Chemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033 Japan.

Yan Wu (Y)

Department of Chemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033 Japan.

Yukiko Matsunaga (Y)

Laboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita-shi, Osaka 565-0871, Japan.

Junichi Takagi (J)

Laboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita-shi, Osaka 565-0871, Japan.

Tomoki Nakashima (T)

Department of Cell Signaling, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University, Tokyo 113-8549, Japan; naka.csi@tmd.ac.jp hsuga@chem.s.u-tokyo.ac.jp.
Japan Agency for Medical Research and Development, Core Research for Evolutional Science and Technology, Tokyo 113-8549, Japan.

Hiroaki Suga (H)

Department of Chemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033 Japan; naka.csi@tmd.ac.jp hsuga@chem.s.u-tokyo.ac.jp.

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Classifications MeSH