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Amino Acids and Peptides. XXIX. Synthesis and Antimetastatic Effects of Peptides and Peptide-Poly(Ethylene Glycol) Hybrids Related to the Core Sequence of the Type III Connecting Segment Domain of Fibronectin.
Bibliographic Information
- Other Title
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- Amino Acids and Peptides-29- Synthesis and Antimetastatic Effects of Peptides and Peptide-Poly(Ethylene Glycol)Hybrids Related to the Core Sequence of the Type 3 Connecting Segment Domain of Fibronectin
- Amino Acids and Peptides.29.Synthesis a
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Description
Peptides (H-Glu-Ile-Leu-Asp-Val-NH2, H-Glu-Ile-Leu-Asp-Val-Pro-Ser-Thr-NH2, H-Arg-Glu-Asp-Val-NH2) and their poly(ethylene glycol)(PEG) hybrids related to the core sequence of the type III connecting segment domain of fibronectin A chain were prepared by the solution method or the solid phase method. Their inhibitory effects on the adhesion and migration of B16-BL6 melanoma cells to fibronectin were assessed in vitro, and their therapeutic potency against tumor metastasis were also examined. Anti-adhesive and anti-migrative effects of the synthetic fibronectin-related peptids were superior to those of their PEG hybrids, so we found that the in vitro bioactivity of peptides decreased by PEGylation. In the in vivo assay, we found that the synthetic peptides containing Glu-Ile-Leu-Asp-Val and Arg-Glu-Asp-Val sequences exhibited an inhibitory effect on the experimental metastasis of B16-BL6 melanoma. Of the synthetic peptides, H-Glu-Ile-Leu-Asp-Val-NH2 exhibited the most potent inhibitory effect. Hybrid formation of Arg-Glu-Asp-Val with poly(ethylene glycol) resulted in potentiation of the inhibitory effect of the parent peptides. A mixture composed of PEG hybrids of Glu-Ile-Leu-Asp-Val, Arg-Glu-Asp-Val and Tyr-Ile-Gly-Ser-Arg dramatically inhibited tumor metastasis.
Journal
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- Biological and Pharmaceutical Bulletin
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Biological and Pharmaceutical Bulletin 19 (12), 1574-1579, 1996
The Pharmaceutical Society of Japan
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Keywords
Details 詳細情報について
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- CRID
- 1390282679598433408
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- NII Article ID
- 110003641121
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- NII Book ID
- AA10885497
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- ISSN
- 13475215
- 09186158
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- NDL BIB ID
- 4099038
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- PubMed
- 8996642
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- Text Lang
- en
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- Article Type
- journal article
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- Data Source
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- JaLC
- NDL Search
- Crossref
- PubMed
- CiNii Articles
- OpenAIRE
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- Abstract License Flag
- Disallowed