Dec, 2019
Identification of active sequences in human laminin α5 G domain.
Journal of peptide science : an official publication of the European Peptide Society
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- Volume
- 25
- Number
- 12
- First page
- e3218
- Last page
- Language
- English
- Publishing type
- Research paper (scientific journal)
- DOI
- 10.1002/psc.3218
Human laminin-511 (α5β1γ1) and its truncated protein, laminin-511 E8 fragment, bind to integrin α6β1 and have been widely used for embryonic stem cell and induced pluripotent stem cell culture under feeder-free conditions. In this study, we focused on human laminin α5 chain G domain, which is thought to be critical for the biological functions of laminin-511, and screened its biologically active sequences using a synthetic peptide library. We synthesized 115 peptides (hA5G1-hA5G115) covering the entire laminin α5 chain G domain and evaluated cell attachment activity using both the peptide-coated plate and peptide-chitosan matrix (peptide-ChtM) assays. Seventeen peptides demonstrated cell attachment activity in the assays. Both hA5G18 and hA5G26-coated plates and hA5G74-ChtMs promoted integrin β1-mediated cell attachment. These findings are useful for the study of molecular mechanisms of laminin-511, and the active peptides have a potential for use as a molecular probe for cell adhesion receptors.
- Link information
- ID information
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- DOI : 10.1002/psc.3218
- ISSN : 1075-2617
- Pubmed ID : 31755207