ArticleACS omega2026
Influence of Structural Features of Peptides on Their Affinity to Cotton Linters Paper.
Article in ACS omega, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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2 authors.
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Abstract
As an alternative to chemical functionalization of cellulose, fusion constructs with carbohydrate-binding modules (CBMs) can be used for the noncovalent immobilization of various compounds and functionalities on cellulose. Smaller cellulose-binding peptides might be used as an alternative, as they are easy to modify and can be produced completely synthetically. To investigate which structural features of peptides promote binding to cotton linters paper, we have established a label-free assay to assess paper affinity. Even though tyrosine residues are essential for the binding of CBMs, we found that the Y/A exchange in peptides did not lead to a reduction in the affinity. This confirms previous assumptions that aromatic structures that are needed to orient CBMs during cellulose binding are less important for smaller, more flexible peptides. We also show that the aromatic fluorophore 5(6)-carboxytetramethylrhodamine (TAMRA), which is sometimes used for peptide labeling, leads to an increase in affinity due to an avidity effect. In addition, we observed that peptides with a
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