ArticleNanomaterials (Basel, Switzerland)2020
The Effect of Oligomerization on A Solid-Binding Peptide Binding to Silica-Based Materials.
Article in Nanomaterials (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 9 citations in OpenAlex.
- Biomedical applications of solid-binding peptides and proteins.Materials today. Bio · 2023Review
- Design of Polypeptides Self-Assembling into Antifouling Coatings: Exploiting Multivalency.Biomacromolecules · 2022Article
- Circular dichroism for secondary structure determination of proteins with unfolded domains using a self-organising map algorithm SOMSpec.RSC advances · 2021Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bifunctional linker-protein G (LPG) fusion protein comprises a peptide (linker) sequence and a truncated form of Streptococcus strain G148 protein G (protein G). The linker represents a multimeric solid-binding peptide (SBP) comprising 4 × 21-amino acid sequence repeats that display high binding affinity towards silica-based materials. In this study, several truncated derivatives were investigated to determine the effect of the SBP oligomerization on the silica binding function of LPG (for the sake of clarity, LPG will be referred from here on as 4 × LPG). Various biophysical characterization techniques were used to quantify and compare the truncated derivatives against 4 × LPG and protein G without linker (PG). The derivative containing two sequence repeats (2 × LPG) showed minimal binding to silica, while the truncated derivative with only a single sequence (1 × LPG) displayed no binding. The derivative containing three sequence repeats (3 × LPG) was able to bind to silica with a binding affinity of K
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