Structural optimization of cyclic peptides that efficiently detect denatured collagen

Koh K. Takita, Kazunori Fujii, Kento Ishii, Takaki Koide

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

To develop a facile method for detecting denatured collagen, we investigated the structure-activity relationship of cyclic collagen-mimetic peptides (cCMPs). Reported cCMP prototypes tend to self-assemble and they must be disassembled just before use. Introducing charge repulsion and a deformation in the peptide backbone structure enabled cCMPs to detect denatured collagen without a pre-treatment for disassembly. Using the optimized cCMP, types I-V collagen were detected by western blotting and denatured collagen fibrils were visualized in a cell culture system.

Original languageEnglish
Pages (from-to)7380-7387
Number of pages8
JournalOrganic and Biomolecular Chemistry
Volume17
Issue number31
DOIs
Publication statusPublished - 2019 Jan 1

Fingerprint

Cyclic Peptides
Structural optimization
collagens
peptides
Collagen
optimization
Peptides
Structure-Activity Relationship
Collagen Type I
Cell culture
pretreatment
Cell Culture Techniques
Western Blotting
prototypes

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry

Cite this

Structural optimization of cyclic peptides that efficiently detect denatured collagen. / Takita, Koh K.; Fujii, Kazunori; Ishii, Kento; Koide, Takaki.

In: Organic and Biomolecular Chemistry, Vol. 17, No. 31, 01.01.2019, p. 7380-7387.

Research output: Contribution to journalArticle

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